Results for "glycerol"

You place a RBC (0.9%) into a 5% sugar solution. Which statement below is false? The RBC is hypotonic to the 5% solution Which is an example of a sensor in a negative homeostatic feedback loop? Chemoreceptor in carotid body For membrane fluidity experiment, the part of the experiment that actually validated that the membrane was fluid was: The labeled antibodies of the human and mouse intermixing An example of primary active transport would be a protein requiring ATP to transport sodium ions across the plasma membrane. True If a red blood cell is put in a solution and it hemolyzes, then the solution is considered to be: Hypotonic If your body temperature goes too high you can denature enzymes in your body. True What does an integrator do in a homeostatic pathway? Measures the signal coming in to a set point and send a signal out to the body Which of the following represents stages of the cell division (mitosis) in the proper sequence? Prophase, metaphase, anaphase, telophase Which is not true for proteins? They are comprised of mostly cellulose What would be a disturbance for blood glucose homeostasis (normal blood glucose set point = 77mg/dL)? A permanent decrease in insulin production from the Islets of Langerhans Dr. Bio measures your total cholesterol and he reports back to you that your level is 300 mg/ 100 ml of plasma. You do what? Eat more oatmeal and flax to increase your HDL level. How do you make an unsaturated fatty acid? Perform a dehydration synthesis reaction on a saturated fatty acid Which is false for antioxidants? They speed up reactions in your body Which molecules do not dissolve in water? Non-polar Which molecule requires a transport protein to get through the plasma membrane (either channel or carrier protein)? Two of the answers are correct Interphase is considered to be part of normal cell division (mitosis). False What is the function of ATP? All of the answers are correct What are the three kinds of lipids? Triglycerides, phospholipids, and steroids When glycerol combines with 3 fatty acids to form a triglyceride (fat), which of the following chemical reactions has occurred? Dehydration Synthesis How can you alter a protein’s shape? More than one answer is correct If a red blood cell is put into a solution and it maintains its shape, then the solution is considered to be: Isotonic Which molecule requires some type of transport protein to get through the plasma membrane? Sodium Ion Cofactors are molecules that activate enzymes. Which is not a cofactor? Mercury The nitrogenous bases found in DNA have complementary paring. Which pair is correct? C-G Which is not true for meiosis? Results in a gamete that is 2N In the diagram below the two solutions are separated by a semi permeable membrane. In which direction will net movement of water occur? From side A to side B Which is not a component of a DNA molecule: Ribose Sugar Phospholipids are similar to fatty acids except for? Phospholipids have a phosphate group Which is not true for cells? They allow diffusion of all molecules If you combine a molecule of glucose and fructose, which statement is true? You have formed sucrose Which is true for enzymes? Activity will increase until the enzyme becomes saturated What method would you use to get glucose into a cell along/down it’s concentration gradient (from high to low)? Facilitated Diffusion Which is not considered an integrator in a negative homeostatic feedback loop? Pancreas Which phase of the cell cycle is where cytokinesis takes place? Telophase What vitamin do we produce by sitting in the sun; it aids in calcium absorption from the small intestine? Vitamin D Why is it important to think about ion dissociation in the body? All the above In what order do you use macromolecules for fuel? Carbohydrates, lipids, proteins Which is false for cholesterol? It can dissolve in water/blood You place a RBC (0.9%) into a 0.5% sugar solution. Which statement below is false? The RBC is hypertonic to the 0.5% solution Which is not a membrane protein function? Protein synthesis Ingesting (eating) excess hydrophilic vitamins, such as vitamin C, results in excess vitamin C being stored in your tissues. False Diffusion is: The movement of molecules from an area of high molecular concentration to an area of low molecular concentration across a selectively-permeable membrane The hormone responsible for glucose uptake/removal from the blood is: Insulin What method would you use to get sodium ions into a cell against sodium’s concentration gradient (from low to high concentration)? Active Transport Which phase of the cell cycle is where the cell is functioning normally or doing its job? Interphase Evidence for mitochondria once being bacteria that our cells engulfed is: It has it’s own DNA Ionic molecules (ie NA+, K+) can diffuse straight through the plasma membrane. True What is the difference between cis and trans fatty acids? Cis fatty acids have hydrogens on the same side of the carbon double bond and trans fatty acids do not Cofactors are molecules that activate enzymes. Where do we get cofactors from? Vitamins found in fruits and vegetables RNA has what nitrogenous base in place of thymine? Uracil Large polar molecules (ie glucose) can diffuse straight through the plasma membrane? False Which lipoprotein is comprised of more protein and less cholesterol so it scavenges for cholesterol in the blood? High density lipoprotein A normal human being has 46 chromosomes (23 pairs/2N/diploid) in each somatic cell (body cell). True The three main compounds digested by the digestive system are? Fats, carbohydrates, and proteins Meiosis is the process in which our sex cells go from 46 chromosomes to 23 single chromosomes. True The effector in any negative feedback loop is usually: An organ/tissue If a red blood cell is put into a solution and it crenates (shrinks), then the solution is considered to be: Hypertonic Which statement is false for glycogen? It is a disaccharide Enzymes aid in digestion by? Lowering the energy required to break food apart Nonpolar molecules (ie CO2) can diffuse straight through the plasma membrane

HOMEOSTASIS Maintaining a stable internal environment respond to stimuli Reacting to changes in the environment reproduce and develop Creating new organisms and growing adapt and evolve Changing over time to better suit the environment INDUCTIVE REASONING Making generalizations based on specific observations DEDUCTIVE REASONING Making specific predictions based on general principles Matter Anything that has mass and takes up space elements Substances that cannot be broken down into simpler substances protons Positively charged particles in the nucleus neutrons Neutral particles in the nucleus electrons Negatively charged particles orbiting the nucleus Atomic Number Number of protons in an atom Isotopes Atoms of the same element with different numbers of neutrons Octet Rule Atoms tend to gain, lose, or share electrons to achieve a full outer shell of 8 electrons molecule Two or more atoms held together by chemical bonds compound A substance consisting of two or more different elements IONIC BONDS Bonds formed by the transfer of electrons COVALENT BONDS Bonds formed by the sharing of electrons reactants Starting materials in a chemical reaction products Ending materials in a chemical reaction WATER solvent Dissolves many substances WATER cohesion & adhesion Water molecules stick to each other and other surfaces WATER high surface tension Water's surface resists being broken WATER high heat capacity Water can absorb a lot of heat without changing temperature WATER heat of vaporization Water requires a lot of energy to evaporate WATER varying density Ice is less dense than liquid water acidic solutions Solutions with a pH below 7 basic solutions Solutions with a pH above 7 pH scale Measures the acidity or basicity of a solution buffers Substances that resist changes in pH Organic Molecules Molecules containing carbon carbon The backbone of organic molecules functional groups Chemical groups attached to carbon that give molecules specific properties Macromolecules Large molecules made up of smaller subunits monomers The individual subunits of a polymer polymers Long chains of monomers Dehydration Synthesis Reaction Joins monomers by removing water Hydrolysis Reaction Breaks polymers by adding water Role of Enzymes Speed up chemical reactions Carbohydrates monosaccharides glucose Simple sugars Carbohydrates disaccharides glycosidic bonds Two monosaccharides joined together Carbohydrates polysaccharides starch glycogen cellulose Many monosaccharides joined together LIPIDS Glycerol & Fatty Acids saturated Fatty acids with no double bonds LIPIDS Glycerol & Fatty Acids unsaturated Fatty acids with double bonds PROTEINS Enzymes Proteins that catalyze chemical reactions PROTEINS amino acids peptide bonds The monomers of proteins, joined together PROTEINS protein structure primary The sequence of amino acids PROTEINS protein structure secondary Local folding patterns (e.g., alpha-helices and beta-sheets) PROTEINS protein structure tertiary The overall 3D shape of a single polypeptide PROTEINS protein structure quaternary The arrangement of multiple polypeptides in a protein conformation The 3D shape of a protein denaturation The unfolding of a protein DNA Deoxyribonucleic acid, the genetic material RNA Ribonucleic acid, involved in protein synthesis ATP Adenosine triphosphate, the energy currency of the cell

Primary adrenal insufficiency = problem at level of adrenal glands Causes? Addison’s disease Pathophys? Autoimmune destruction of the adrenal glands Associated with hyperpigmentation POMC is precursor to both ACTH and MSH PAI → lack of negative feedback → high ACTH Lab findings? ACTH high Aldosterone low Destruction of zona glomerulosa Renin high Hypotension → RAAS activation Electrolytes Na+ low, K+ high CBC Eosinophils high Pathophys? Glucocorticoids → eosinophil apoptosis. Lack of glucocorticoids cause eosinophilia. Dx? Cosyntropin testing → no rise in cortisol Adrenal glands aren’t working, so no response to ACTH. Tx? prednisone/hydrocortisone/dexamethasone + fludrocortisone (mineralocorticoid) Stress-dose steroids for surgery, serious illness, etc. Secondary adrenal insufficiency = problem at level of pituitary, reduced ACTH release Causes? MC is prolonged steroid use → ACTH suppression Sheehan’s syndrome (infarction of pituitary) pregnancy Pituitary tumors (ACTH-producing tumor) Lab findings? ACTH low Anterior pituitary is being inhibited Aldosterone normal Zona glomerulosa under control of RAAS system Renin normal Electrolytes Na+ & K+ unaffected (Aldosterone levels are normal) CBC Neutrophilia due to demargination (if pt was recently taking steroids) Dx? Cosyntropin testing → rise in cortisol Adrenal gland is functional Tx? Glucocorticoids Do not need to replace mineralocorticoids since adrenals are functional and aldosterone is under RAAS control Stress-dose steroids for surgery, serious illness, etc. AI with a history of nuchal rigidity and purpuric skin lesions → Waterhouse-Friedrichson syndrome Pathophys? AI 2/2 hemorrhagic infarction of the adrenal glands in the context of Neisseria meningitidis infection Adrenal synthesis enzymes If the enzyme starts with 1 → HTN (high mineralocorticoids) and hypokalemia If the second # is 1 → virilization (high androgens) E.g. 11-beta hydroxylase deficiency → HTN & virilization E.g. 21 hydroxylase deficiency → virilization only E.g. 17-alpha hydroxylase deficiency → HTN only B12 deficiency Where does B12 come from? Animal products VS folic from plants Physiology R factor in saliva binds to B12 and protects it from acidity in the stomach. R factor protector -B12 travels to the duodenum. Parietal cells produce intrinsic factor, which travels to the duodenum. Pancreatic enzymes cleave B12 from R factor and B12 then binds IF. B12-IF complex is reabsorbed in the terminal ileum Reabsorption where? Terminal ileum Causes of B12 deficiency Extreme vegan Pernicious anemia Pancreatic enzyme deficiency Cystic Fibrosis Can’t cleave B12 from R factor Crohn’s Affects terminal ileum Lab markers Homocysteine HIGH MethlyManoicAcid HIGH Presentation? Megaloblastic anemia Subacute combined degeneration (of dorsal columns + lateral corticospinal tract) Peripheral neuropathy Dx of pernicious anemia? anti-IF Ab Folate deficiency Where does folate come from? Leafy things Causes of folate deficiency Poor diet (e.g. alcoholics, elderly) Phenytoin Lab markers Homocysteine HIGH MMA normal Presentation? Megaloblastic anemia Prophylaxis in HIV+ patients CD4 < 200 → PCP TMP-SMX, inhaled pentamidine, dapsone, atovaquone CD4 < 100 → Toxoplasm Treat: TMP-SMX CD4 < 50 → MAC Treat: Azithromycin If live in endemic area, CD4 < 250 → Coccidioides Immitis E.g. Arizona, Nevada, Texas, California Treat: Itraconazole If live in endemic area, CD4 < 150 → Histoplasma Capsulatum E.g. Kentucky, Ohio, Missouri Treat: Itraconazole Diabetes insipidus Dx? Water deprivation test Measure serum osmolality & urine osmolality Deprive pt of water Remeasure serum osmolality & urine osmolality If urine osmolality doesn’t go up → suspect DI Central DI → deficiency of ADH Pathophys? Supraoptic nucleus not making enough ADH Dx? Give desmopressin → urine osmolality increases significantly Nephrogenic DI → kidneys are not responding to ADH Dx? Give desmopressin → urine osmolality doesn’t change much Tx? Hydrochlorothiazide Unless 2/2 lithium, use amiloride or triametere Causes? Lithium SSRIs Carbamazepine Demeclocycline Tx of normovolemic hypernatremia? D5W to correct free water deficit Divine says NS, but most other resources I found said correct free water deficit Tx of hypovolemic hypernatremia? Give NS first until normal volume, then give D5W Consequence of correcting hypernatremia too rapidly? Cerebral edema Osteoarthritis Presentation? Old person with joint pain that gets worse throughout the day Risk Factr? Obesity vs decreases osteoporosis Imaging findings? Joint space narrowing Subchondral sclerosis Subchondral cysts Osteophytes Arthrocentesis findings? <2000 cells Tx? 1st line acetaminophen 2nd line NSAID (e.g. naproxen) 3rd line joint replacement surgery Returned from a business conference 1 week ago + Fever + Nonproductive cough + Abdominal pain + Hyponatremia → Legionella Dx? Urine antigen Tx? FQ or macrolide MaCroLide mnemonic = Mycoplasma, Chlamydia, Legionella What are the common causes of atypical PNA? Mycoplasma, Legionella, Chlamydia MC cause? Mycoplasma CXR findings? Interstitial infiltrates HY associations C. Psittaci → birds C. Burnetii → cows, goats, sheet Mycoplasma → college student w/ walking pneumonia Midsystolic click heard best at the apex. → mitral valve prolapse “Stenosnap & Proclick” Risk Factor? Connective tissue disease Marfarn Ehlers-Danlos ADPKD bilateral renal masses Classic demographic? Young woman psychiatric Pathophys? Myxomatous degeneration MVP vs aortic dissection: cystic medial necrosis Exam maneuvers Anything that increase amount of blood in LV → murmur softer Increase preload Increase afterload Anything that decreases amount of blood in LV → murmur louder Dx? Echo Scaly, itchy skin with yellowish crusting in the winter. → seborrheic dermatitis Tx? Topical antifungals e.g. ketoconazole or selenium sulfide shampoo Classic disease distribution? Hair → e.g. cradle cap Eyebrows Episodic/intermittent HTN + HA → pheochromocytoma Genetic disease associations MEN2A MEN2B VHL in brain (hemangioma) NF-1 growth in skin Pathophys? Catecholamine-secreting tumor Location? Adrenal medulla Posterior mediastinum Organ of Zuckerkandl (chromaffin cells along the aorta) Dx? 1st step: urine metanephrines If elevated → CT abdomen If nothing found on CT → MIBG scan Tx? Alpha blocker (e.g. phenoxybenzamine, phenotaline) THEN beta blocker Most common cause of a Lower GI Bleed in the elderly → diverticulosis Dx? Colonoscopy or barium enema Recall that you acutely do a CT scan for diverticulitis, then 6 weeks later colonoscopy to r/o cancer Ppx? Eat fiber Megaloblastic anemias Blood smear findings? Hypersegmented neutrophils MCV > 100 Classic patient demographic with folate deficiency? Alcoholics Elderly person with poor nutrition Folate synthesis inhibitors Pt with molar pregnancy → methotrexate Pulmonary issue? Pulmonary fibrosis HIV+ pt with ring-enhancing lesions → pyrimethamine-sulfadiazine Pyrimethamine inhibits DHFR AIDS pt on ppx for toxo → TMP-SMX TMP inhibits DHFR Use of leucovorin? Rescue bone marrow in setting of methotrexate toxicity Mechanism? Folinic acid analog CMV presentations Esophagitis → linear ulcers Colitis → post-transplant pt Retinitis → HIV pt with CD4 < 50 Congenital CMV → periventricular calcifications + hearing loss calcifications elsewhere → toxo Histology? Owl’s eye intranuclear inclusions Tx? Gancicyclovir Resistance? UL97 kinase mutation Tx for resistance? foscarnet CD4 < 200 + severe peripheral edema + frothy urine. → FSGS in HIV pt Variant classic in HIV+ pts? Collapsing variant Tx? Steroids + cyclophosphamide + ACE-I Indinavir AE? Kidney stones triad of fever, rash, and eosinophiluria → acute interstitial nephritis Drugs cause? Penicillins Tx? Stop the drug! Can add steroids if severe Vitamin D metabolism Liver converts Vit D to calcidiol (25OH-Vit D). Calcidiol goes to kidney. Alpha-1 hydroxylase converts calcidiol to calcitriol (1,25-OH Vit D). Common causes of Vitamin D deficiency CKD → 1-alpha hydroxyalse deficiency Liver disease → can’t make calcidiol CF → malabsorption Crohn’s → malabsorption Osteomalacia vs Rickets Osteomalacia in adults Rickets in kids Tx? Calcium + vit D Lab findings? Ca++ low Phos low Low in liver disease High in kidney disease (kidneys can’t get rid of phos) PTH high (2ary hyperpara) vs liver dx PTH low Alk phos Aspiration pneumonia Risk Factor? Alcoholism Dementia Neuromuscular problems (e.g. MG, ALS) Bugs? Anaerobes foul smelling Bacteroides FUsobacterium Peptostreptococcus Klebsiella → currant jelly sputum alcoholic Tx? Clindamycin CURB-65 criteria Purpose? Who to admit Cutoff? 2+ → hospitalize C = confusion U = uremia (BUN > 20) R = RR > 30 B = BP < 90/60 Age > 65 Drugs commonly used in PNA treatment Ceftriaxone Levofloxacin fluoroquinolone Macrolides - great for atypical PNA Pharmacological management of pulmonary arterial HTN Endothelin antagonists Bosentan ambrisentan PDE-5 inhibitors Sildenafil Tadalafil Prostacyclin analogs Iloprost Epoprostenol Treprostinil Causes? Young female → idiopathic PAH Mutation? BMPR2 55 yo F presents with a 5 week history of a rash on her forehead. PE reveals scaly macules with a sandpaper texture. → actinic keratosis Risk Factor? Sun exposure Tx? Topical 5-FU Possible dangerous sequelae? Squamous cell carcinoma Most likely disease sequelae? Resolution 1ary hyperparathyroidism 2ary hyperparathyroidism 3ary hyperparathyroidism Autonomous PTH production Causes? Adenoma Parathyroid hyperplasia PTH high Ca++ high Phos low Low Ca++ → PTH production Causes? CKD PTH high Ca++ low Phos high PTH production despite normalized of Ca++ levels Causes? CKD s/p transplant PTH high Ca++ high Phos low Tx? Parathyroidectomy (remove 3.5 glands) Cinacalcet (CSR modulator) Hypercalcemia Presentation? bones, stones, groans, psychic overtones Tx? 1st step: Normal Saline Hypercalcemia of malignancy → bisphosphonates EKG finding? Shortened QT Periumbilical pain that migrates to the right lower quadrant. → appendicitis PE findings? McBurney’s point tenderness Psoas sign (flex hip pain) Obturator sign (pain with internal rotation of hip) Rovsing’s sign (palpation of LLQ → pain in RLQ) Dx? CT scan Pregnant → US Kid → US Tx? Surgery Classic drug and viral causes of aplastic anemia. Drugs? Carbamazepine Chloramphenicol Viral? Parvovirus B19 (single stranded DNA virus) Fanconi anemia Pathophys? Problems with DNA repair Fanconi anemia vs Fanconi syndrome Fanconi anemia → cytopenias + thumb anomalies + short stature + cafe-au-lait spots Fanconi syndrome → type 2 RTA (proximal) CD4 count of 94 + MRI revealing ring enhancing lesions in the cortex → toxoplasmosis Tx? Pyrimethamine-sulfadiazine Rescue agent for pt who becomes leukopenic with treatment? leucovorin Who should get steroids? Increased ICP For PCP pneumonia: O2 sat < 92 PaO2 < 70 A-a gradient > 35 Ppx? TMP-SMX for CD4 < 100 Congenital toxo Hydrocephalus Chorioretinitis Intracranial calcifications Classic methods of transmission? handling cat litter Lupus nephritis Associated autoantibody? anti-dsDNA Classic “immunologic” description? “Full house” pattern Tx? Steroids + cyclophosphamide Osteoporosis Screening population? women > 65 Screening modality? DEXA scan Dx? T-score < -2.5 Risk Factor? Postmenopauseal Low BMI Smoking Alcohol Preventive strategies? Weight bearing exercise Smoking cessation Reduce alcohol consumption Tx? 1st line: bisphosphonates + Ca/Vit D supplementation Raloxifene (SERM) Agonist in bone Blocker Antagonist in breast Classic locations of osteoporotic fractures Vertebral compression fracture Hip fracture Name the PNA Red currant jelly sputum. → Klebsiella Rust colored sputum. → Strep pneumo PNA in an alcoholic. → Klebsiella Post viral PNA with a cavitary CXR lesion. → Staph aureus PNA in a patient that has chronically been on a ventilator. → Pseudomonas MC cause of Community Acquired Pneumonia. → Strep pneumo Pharmacological management of MRSA. Vancomycin Clindamycin Linezolid Ceftaroline (5th gen cephalosporin) Tigecycline, tertracycline Pharmacological management of Pseudomonas. Ceftazidime (only 3rd gen cephalosporin) Cefepime (4th gen cephalosporin) Pip-tazo Fluoroquinolones Carbapenems Aztreonam Aminoglycosides JVD and exercise intolerance in a patient with a recent history of an URI. → dilated cardiomyopathy 2/2 viral myocarditis MC cause? Coxsackie B VS Coxsackie A: Hand foot mouth dx Drug causes myocarditis Clozapine Anthracyclines Prevention? Dexrazoxane (iron chelator) Trastuzumab reversible tx for breast cancer Classic cause in a patient with recent history of travel to S. America? Chagas T. Cruzi Potential sequelae? Achalasia Dilated cardiomyopathy Megacolon (2/2 degeneration of myenteric plexus) Massive skin sloughing (45% BSA) in a patient that was recently started on a gout medication? TEN Dx? <10% BSA → SJS >30% BSA → TEN Tx? STOP the drug IVF Topical abx to prevention infection Tetany and a prolonged QT interval in a patient with recent surgical treatment of follicular thyroid carcinoma. → hypocalcemia due to removal of parathyroids Recurrent viral infections + QT prolongation + tetany → DiGeorge syndrome Pathophys? Failure of development of 3rd/4th pharyngeal pouches Trousseau and Chvostek signs. Trousseau → inflation of BP cuff causes carpopedal spasm Chvostek → taping on cheek causes facial muscle spasm Hypocalcemia that is refractory to repletion → consider hypomagnesemia Electrolyte/drug causes of prolonged QT intervals Electrolytes? Hypocalcemia Hypomagnesemia Hypokalemia Drugs? Macrolides FloroQunlones Haloperidol Ondensatron Methadone Hypoalbuminemia and Ca balance Hypoalbumenia → decrease in total body Ca++, no change in ionized Ca++ Drop of 1 in albumin → add 0.8 to Ca++ Abdominal pain radiating to the back → acute pancreatitis Causes? #1 = Gallstones #2 = Alcohol Hypertriglyceridemia Hypercalcemia Scorpion sting Handlebar injuries Lab markers? Lipase - most sensitive Amylase Physical exam signs in pancreatitis. Cullen’s sign = periumbilical ecchymosis Grey Turner sign = flank ecchymosis Tx? NPO + IVF + pain control Meperidine is a good agent because it doesn’t cause sphincter of Oddi spasms Management of gallstone pancreatitis Dx? US then ERCP Tx? DELAYED cholecystectomy What if the patient becomes severely hypoxic with a CXR revealing a “white out” lung? ARDS noncardiogenic pulm edema PCWP? <18 mmHg NORMAL 20 yo M with red urine in the morning + hepatic vein thrombosis + CBC findings of hemolytic anemia. → paroxysmal nocturnal hemoglobinuria Pathophys? Defect in GPI anchors, which attach CD55 and CD59 to cell (they prevent complement from destroying RBC) Sleep → hypoventilation → mild respiratory acidosis → activation of complement cascade Gene mutation? PIGA Dx? Flow cytometry Tx? Eculizumab (terminal complement inhibitor) Vaccine required? pnemococal Neisseria meningitidis Chronic diarrhea and malabsorption in a HIV+ patient + detection of acid fast oocysts in stool. → cryptosporidium parvum Acid-fast organisms Cryptosporidium TB MAC Nocardia Dx? Stool O&P Tx? Nitazoxanide Route of transmission? Contaminated water Muddy brown casts on urinalysis in a patient with recent CT contrast administration (or Gentamicin administration for a life threatening gram -ve infection) → Acute Tubular Necrosis Woman with morning joint stiffness > 1 hr → Rhematoid Arthritis. Antibodies? Rheum Factor (IgM against IgG) anti-CCP - more specific HLA? DR4 Pathophys? IgM constant region activates complement → inflammation → formation of pannus (hypertrophied synovium) → damage to cartilage and bone Caplan syndrome = RA + pneumoconiosis Felty syndrome = RA + neutropenia + splenomegaly (“RANS”) Classic hand/finger findings/distribution? MCP & PIP joints of hands (DIP joints spared) Imaging findings? Symmetric joint space narrowing Tx? Methotrexate (DMARDs) If no response → TNF alpha inhibitor (e.g. infliximab) Required testing prior to starting methotrexate? PFTs Required testing prior to starting infliximab? TB Hep B/Hep C Differentiating Strep pharyngitis from Infectious Mononucleosis LND distribution Anterior cervical → Strep Posterior cervical → Mono Disease onset Acute → Strep Over weeks → Mono Organ involvement Splenomegaly → Mono Pt with sore throat takes amoxicillin and gets rash → mono NOT allergic rxn! CENTOR criteria C = absence of Cough E = tonsillar Exudates N = nodes/anterior cervical lymphadenopathy T = temp (fever) OR <15 → +1 >=45 → -1 Using CENTOR score 0/1 → don’t test, don’t treat 2/3 → rapid antigen test Positive → treat Negative → throat culture 4/5 → treat empirically Tx of Strep pharyngitis? Amoxillcin If PCN allergic → azithromycin Potential sequelae of Strep pharyngitis RF - preventable with abx PSGN Endocarditis MC cause of endocarditis? IVDU Bug? Staph aureus Valve? tricuspid Prosthetic valve endocarditis Bug? Staph epidermidis Endocarditis after dental procedure? Viridans group streptococci Strep viridans, Strep mitis, Strep mutans, Strep sanguineous Patient with malar rash and echo showing vegetations on both sides of the mitral valve → Libman-Sacks endocarditis Presentation? Fever + night sweats + new murmur Splinter hemorrhages Roth spots (retinal hemorrhages) Painless Janeway lesions + painful Osler nodes (immune phenomenon) Dx? 1st step: blood cultures TEE Tx? Abx that include Staph aureus coverage (e.g. vancomycin) for WEEKS Bugs implicated in culture negative endocarditis HACEK H = haemophilus A = actinobacillus C = cardiobacterium E = eikenella K = kingella Coxiella burnetii Blood cultures in a patient with endocarditis reveal S. Bovis (or S. Gallolyticus bacteremia). NBS? Colonoscopy Who needs antibiotic prophylaxis? Hx endocarditis Prosthetic valve Unrepaired cyanotic congenital dz Heart transplant with valve dysfunction Erythematous salmon colored patch with silvery scale on the elbows and knees. → psoriasis Tx? Topical steroids If this patient presents with joint pain (especially in the fingers)? Psoriatic arthritis Imaging? Pencil-and-cup deformity Tx? NSAIDs T of 104 + tachycardia + new onset Afib in a patient with a history of Graves disease. → thyroid storm Lab findings? TSH low T3/T4 high Tx? 1st step: propranolol 2nd step: PTU Then: Prednisone Potassium iodide (Lugul’s solution) Wolff-Chaikoff effect → large amounts of iodine inhibit thyroid hormone synthesis Biopsy revealing tennis racket shaped structures in cells of immune origin. → Langerhans cell histiocytosis Electron microscopy? Birbeck granules (tennis rackets) Marker? S100 Small bowel obstruction in a HIV patient with purple macules on the face, arms, and lower extremities. → Kaposi’s sarcoma Bug? HHV8 Tx? HAART Pathophys of vascular lesions? Overexpression of VEGF Fever + rash + eosinophiluria 10 days after a patient started an antistaphylococcal penicillin. → acute interstitial nephritis Tx? STOP drug + steroids SLE SOAP BRAIN MD S = serositis O = oral ulcers A = arthritis P = photosensitivity B = blood disorders (cytopenias) R = renal A = ANA/anti-dsDNA I = immunologic N = neurologic findings M = malar rash D = discoid rash Type 2 vs 3 HSRs in lupus Type 2 → cytopenias Type 3 → all other manifestations Lupus Ab? ANA anti-dsDNA anti-Smith Lupus nephritis → full house pattern on IF Antiphospholipid antibody syndrome → recurrent pregnancy losses Pathophys? Thrombosis of the uteroplacental arteries. MC cause of death in lupus patients? What I’ve read recently: CV disease Per Divine: Treated → infection Untreated → renal dz Also 40x risk MI Endocarditis in lupus pt? Libman-Sacks endocarditis Neonatal 3rd degree heart block → neonatal lupus Maternal autoimmune dz? Sjogren’s SLE Ab? anti-SSA/anti-Ro anti-SSB/anti-La Tx? Steroids Cyclophosphamide Hydroxychloroquine → good for skin lesions Pulmonary abscesses Bugs? Staph Anaerobes Klebsiella RF? Alcoholism Elderly Post-viral pneumonia MC location of aspiration pneumonia? Superior segment of RLL Chest pain worsened by deep inspiration and relieved by sitting up in a patient with a recent MI or elevated creatinine or URI or RA/SLE. → pericarditis EKG findings? Diffuse ST elevations + PR depression PE finding? Friction rub (“scratchy sound on auscultation”) A few days after MI → fibrinous pericarditis Weeks after MI → Dressler’s Tx? NSAIDS Consider adding on colchicine Cardiac tamponade Beck’s triad = hypotension + JVD + muffled heart sounds EKG findings? Electrical alternans Type of shock? Obstructive cardiogenic (Amboss) CO low SVR high PCWP high Tx? Pericardiocentesis or pericardial Pearly lesion with telangiectasias on the ear in a farmer. → Basal Cell Carcinoma MC type skin cancer Location? Upper lip Dx? Biopsy Tx? Mohs surgery Cold intolerance in a 35 yo white F → hypothyroidism MC cause? Hashimoto’s Histology? lymphoid follicles w/ active germinal centers Lab findings? TSH high T3/T4 low Ab? anti-TPO Anti-thyroglobulin HLA? DR3/DR5 Tx? Levothyroxine Future complication? thyroid lymphoma Massive hematemesis in a patient with a history of chronic liver disease. → ruptured varices Pathophys? L gastric vein has anastomosis with azygos veins. Increased portal pressure → backward flow from L gastric veins to azygous vein (which empties into SVC). Acute tx? IVF + octreotide + ceftriaxone/cipro + EGD w/ ligation/banding Do NOT give a beta blocker for acute tx Prophalaxsis? Beta blocker + spironolactone Other manifestations of elevated portal pressures Caput medusa Internal hemorrhoids Tx for cirrhotic coagulopathies? FFP If uremia → give desmopressin Note: Desmopressin = ADH analog → so, it can cause AE of hyponatremia 2/2 SIADH Hemophilia A Pathophys? deficiency of factor 8 Inheritance? XLR Coag labs? Bleeding time normal PTT HIGH b/c clotting problem PT normal Hemophilia B Pathophys? deficiency of factor 9 Inheritance? XLR Coag labs? Bleeding time normal PTT HIGH PT normal Hemophilia C Pathophys? deficiency of factor 11 Inheritance? AR Coag labs? Bleeding time normal PTT HIGH PT normal Bernard Soulier Syndrome Pathophys? Deficiency of GpIb Coag labs? Bleeding time HIGH PTT normal PT normal Glanzmann Thrombasthenia Pathophys? Deficiency of GpIIbIIIa Coag labs? Bleeding time HIGH PTT normal PT normal Von Willebrand’s disease Pathophys? Deficiency of vWF Inheritance? AD Coag labs? Bleeding time HIGH PTT HIGH vWF is a protecting group for factor 8 PT normal ITP Pathophys? Ab against GpIIbIIIa Classic pt? Pt with SLE Tx? Observation Steroids IVIG Splenectomy TTP Pathophys? Deficiency in ADAMTS13 enzyme → cannot cleave vWF multimers → activation of platelets → thrombosis → thrombocytopenia Presentation? microangiopathic hemolytic anemia + thrombocytopenia + renal failure + fever + neurologic problems Tx? Plasma exchange transfusion****** HUS Bugs? Shigella or E. coli O157:H7 Presentation? Fever+ microangiopathic hemolytic anemia + thrombocytopenia + renal failure + neurologic Platelet deficiency vs coagulation factor bleeds Platelet deficiency → mucosal bleeds, petechiae, heavy menses Coag factor deficiency bleeds → hemarthrosis Why do patients with CKD develop coagulopathy? Uremia → platelet dysfunction Tx? Desmopressin Note: Desmopressin = ADH analog → so, it can cause AE of hyponatremia 2/2 SIADH Exercising caution with transfusion in patients with Bernard Soulier syndrome Do NOT give transfusion that includes platelets They can have an anaphylactic rxn to GpIb (since they don’t have GpIb) Oropharyngeal candidiasis. RF? HIV Chronic ICS use TNF inhibitor Micro finding? Germ tubes at 37 C Tx oral candidiasis? Nystatin swish-and-swallow Tx invasive candidiasis? Amphotericin B Prevention of Amphotericin B toxicity? Liposomal formulation Pleural effusions Light’s criteria (must meet all 3 to be considered transudative!) LDH < 2/3 ULN LOW Pleural LDH/serum LDH < 0.6 LOW Pleural protein/serum protein < 0.5 LOW Causes of transudative effusion CHF Cirrhosis Nephrotic syndrome Note: Per UW 2021: Mechanism of transudate effusion? Decreased pulmonary artery oncotic pressure, e.g. hypoalbuminemia in nephrotic syndrome Increased pulmonary capillary hydrostatic pressure, e.g. volume overload in heart failure Causes of exudative effusion Malignancy Cancer Parapneumonic effusion Tb Note: Per UW 2021: Mechanism of exudate effusion? Inflammatory increased in vascular permeability of membrane (increased flow of interstitial edema into pleural space) Unique cause of both transudative & exudative effusions? PE Classic Pleural Effusion findings? Decreased breath sounds Dullness to percussion Decreased tactile fremitus Tx? Chest tube Chylothorax = lymph in the pleural space Pathophys? Obstruction of thoracic duct or injury to the thoracic duct Pleural fluid findings? High Triglycerides Holosystolic murmur heard best at the apex with radiation to the axilla in a patient with a recent MI. → mitral regurg 2/2 papillary muscle rupture Dx? Echo Why widely split S2? Aortic valve is closing earlier (LV is emptying into both aorta & LA) Maneuvers that increase intensity Increase preload (putting more blood in that can be regurgitated) Increase afterload Decubitus ulcers RF? Elderly Paraplegic Fecal/urinary incontinence Poor nutrition Staging Stage 1 = non-blanchable erythema Tx? Repositioning q2hrs Stage 2 = loss of epidermis + partial loss of dermis Tx? Occlusive dressing superficial Stage 3 = involves entire dermis, extending to subQ fat Does NOT extend past fascia Tx? Surgical debridement Stage 4 = muscle/tendon/bose exposed Tx? Surgical debridement General tx strategies? Repositioning + good nutritional support Marjolin’s ulcer = non-healing wound that is actually squamous cell carcinoma T1DM Pathophys? Autoimmune destruction of pancreas Ab? anti-GAD 65 (glutamic acid decarboxylase) anti-IA2 (islet tyrosine phosphatase 2) Islet cell autoantibodies Insulin autoantibodies Dx? A1c > 6.5% (twice) Fasting BG >= 126 (twice) Oral glucose tolerance test >= 200 (twice) Sxs of DM + random glucose > 200 Tx? Long-acting insulin + mealtime insulin Long-acting Glargine Detemir Rapid-acting Lispro Aspart Glulisine 3 HY complications Nephropathy Retinopathy & cataracts Neuropathy Chronic DM care A1c q3 months Foot exam annually Eye exam annually Microalbumin:Cr ratio annually Nephroprotection in DM? ACE-I GI bleed algorithm 1st step: ABCs + 2 large-bore IVs + IVFs 2nd step: NG lavage Clear fluid → go deeper Blood → UGIB → upper endoscopy Bilious fluid → have ruled out UGIB → proceed to colonoscopy See source → intervene as needed See nothing → CT angiography for large bleed Tagged RBC scan for smaller bleed Antiplatelet Pharmacology Aspirin Mechanism? Irreversibly inhibits COX-1 and COX-2 Clopidogrel/ticlopidine = P2Y12 (ADP receptor) blockers Mechanism? Inhibit platelet activation Abciximab/eptifibatide/tirofiban = GpIIbIIIa receptor blockers Mechanism? Inhibit platelet aggregation Ristocetin cofactor assay Issues with adhesion step → abnormal result Abnormal ristocetin cofactor assays: Von Willebrand disease Bernard Soulier disease Normal ristocetin cofactor assay: Glanzmann Thrombasthenia Von Willebrand disease effects on PTT? Increased Pathophys? vWF is a protecting group for Factor 8. Treatment of VWD? Desmopressin Mechanism? Increases release of vWF from Weibel-Palade bodies of endothelial cells Note: Desmopressin = ADH analog → so, it can cause AE of hyponatremia 2/2 SIADH HSV1 vs HSV2. Oral herpes → HSV1 Genital herpes → HSV2 Dx? PCR (most up-to-date) Tzanck smear (outdated, not very sensitive, nonspecific) → intranuclear inclusions Brain area affected by HSV encephalitis? Temporal lobes CSF findings in HSV encephalitis? RBCs******* Tx herpes encephalitis? Acyclovir AE? Crystal nephropathy Can’t see, can’t pee, can’t climb a tree. → reactive arthritis HLA? B27 Classic bug? Chlamydia Tx? steroids Need abx? Only if ongoing infection Can’t see, can’t pee, can’t hear a bee → Alport syndrome Inheritance? X-linked dominant Tx of NG & CT NG → treat empirically for both → ceftriaxone + azithro/doxy CT → azithro/doxy Hypovolemic Septic Neurogenic Cardiogenic CO low PCWP low SVR high*** CO high PCWP normal SVR low Tx? norepi CO low SVR low CO low PCWP high*** SVR high*** Tx anaphylactic shock? epinephrine Melanomas ABCDE A = asymmetry B = irregular borders C = color variation D = diameter > 6 mm E = evolving Dx? Full-thickness biopsy Excisional for small lesions Punch for larger lesions Most important prognostic factor → Breslow depth DM pharmacology Lactic acidosis → metformin Decreases hepatic gluconeogenesis → metformin Hold before CT w/ contrast → metformin Weight gain → sulfonylureas & TZDs (-glitizones) Diarrhea → acarbose & migliton Inhibits disaccharidases (can’t reabsorb disaccharides) Recurrent UTIs → SGLT-2 inhibitors Weight loss → GLP-1 agonists (e.g. liraglutide, exenatide) & DPP4 inhibitors (-gliptins) Contraindicated in pt with HF → TZDs PPAR-gamma receptor found in kidney → water retention Contraindication in pt with MTC → GLP-1 agonists Biggest risk of hypoglycemia? Sulfonylureas RF esophageal adenocarcinoma Barrett’s esophagus RF esophageal squamous cell carcinoma Smoking Drinking Achalasia Location esophageal adenocarcinoma? Lower 1/3 Location esophageal squamous cell carcinoma? Upper 2/3 MC US? Adenocarcinoma MC worldwide? Squamous cell carcinoma Presentation? Dysphagia to solids → dysphagia to liquids Dx? EGD Staging? CT scan or esophageal US Factor V Leiden Pathophys? Resistance to protein C Dx? Activated Protein C resistance assay Patient needs super large doses of heparin to record any changes in PTT → AT-III deficiency Recall that heparin is a AT-III activator 35 yo with a hypercoagulable disorder that does not correct with mixing studies. → antiphospholipid antibody disorder Anaphylaxis in a patient with a long history of Hemophilia A → Ab against factor 8 that cause type 1 HSR with transfusion Hx of hemophilia, diagnosed 5 years ago. Before you would give them factor 8 concentrate and PTT would normalize. Now they’re requirizing larger doses of factor 8 to normalize PTT. → inhibitor formation (antibodies against clotting factors) Skin necrosis with Warfarin → protein C/S deficiency Prothrombin G20210 mutation → overproduction of factor II Rash in dermatomal distribution → VZV infection Contraindications to VZV vaccination? Pregnant woman Kid < 1 year Severe immunosuppression (e.g. HIV with CD4 < 200) Tx? Acyclovir If resistant, foscarnet Tzanck smear findings? Intranuclear inclusions Shingles vaccination guidelines? Adults over 60 #1 cause of ESRD in the US → DM nephropathy Histology? Kimmelsteil-Wilson nodules #2 cause of ESRD in the US → hypertensive nephropathy Pt with BP 240/150. How fast should you lower BP? 25% in first 24 hrs Drugs for hypertensive emergencies? Nicardipine Clevidipine Nitroprusside AE? Cyanide poisoning Tx? Amyl nitrate + thiosulfate OR hydroxocobalamin Labelol Renal protective medications in patients with DKD or hypertensive nephropathy? ACE-I Anemia + Cranial Nerve deficits + Thick bones + Carbonic Anhydrase 2 deficiency + Increased TRAP + Increased Alkaline Phosphatase. → osteopetrosis Pathophys? Carbonic anhydrase is defective → osteoclasts cannot produce acid to resorb bone Tx? IFN-gamma Osteoclasts are a specialized macrophage IFN-gamma is an activator of macrophages Clinical diagnostic criteria for Chronic Bronchitis Diagnostic criteria? 2 years 3 months/year of chronic cough PFT findings FEV1 low FEV1/FVC ratio low RV high TLC high Which PFT market can differentiate CB from emphysema? DLCO DLCO normal → CB DLCO low → emphysema ****** Tx acute exacerbation? Abx + bronchodilators + corticosteroids (“ABCs”) Prevention? Stop smoking! Afib #1 RF? Mitral stenosis #1 RF MS? Rheumatic fever #1 RF CAD and AAA: smoking #1 RF stroke and aortic dissection: HTN MC arrhythmia in hyperthyroidism → Afib MC site of ectopic foci in Afib → pulmonary veins EKG findings? “Irregularly irregular” + no P waves Location of emboli formation? LA appendage Who should be cardioverted back to sinus rhythm? New onset (<48 hrs) Afib Anticoagulated for 3 weeks + TEE negative for clot Afib that’s refractory to medical therapy Afib & HDUS Q on T phenomenon? Depolarization during T wave (repolarization) can cause QT prolongation → Torsades → death Prevention? SYNCHRONIZED cardioversion Tx? Rate control Beta blockers ND-CCB (e.g. verapamil, diltiazem) Rhythmic control Amiodarone Reducing stroke risk in Afib? Anticoagulation for CHA2DS2VASc score >= 2 Anticoagulation options Valvular cause (e.g. MS) → warfarin Any other cause → warfarin or NOAC (apixiban) Reversal of AC Warfarin → Vit K, four-factor PCC Heparin → protamine sulfate Dabigatran → idarucizumab Crusty, scaly, ulcerating lesion with heaped up borders → squamous cell carcinoma Classic location? Below Lower lip Precursor lesion? Actinic keratosis What if it arises in a scar or chronic wound? Marjolin ulcer Hypothermia + hypercapnia + non pitting edema + hyponatremia + HR of 35 + hypotension in a patient with a history of papillary thyroid cancer → myxedema coma Tx? Levothyroxine + steroids Lab findings? TSH high T3/T4 low LDL high Acute onset “dermatologic” breakout in a patient with a recent history of weight loss and epigastric pain. → Leser–Trélat sign associated with visceral malignancy pancreatic cancer Lymph node associations Supraclavicular → Virchow’s node Periumbilical → Sister Mary Joseph What are mets to the ovaries called? Kruckenberg tumor Classic bug associated with gastric cancer? H. pylori (MALToma) Classic histological finding in the diffuse type of gastric cancer? Signet ring cells RBCs without central pallor + elevated MCHC + anemia. → hereditary spherocytosis Inheritance? AD Pathophys? Deficiency of spectrin, ankyrin, or band 3.2 Intravascular or extravascular hemolysis? Extravascular (RBCs bound by IgG, attacked by splenic macrophages) Dx? Osmotic fragility test Eosin-5-maleimide Acidified glycerol lysis test Tx? Splenectomy Post-splenectomy preventative care? Strep pneumo Hinflue vaccine Neisseria Septic shock Hemodynamic parameters CO high SVR low PCWP normal MvO2 high Tx? IVF + norepi + broad-spectrum abx (cover MRSA + Pseudomonas) E.g. vanc + pip-tazo E.g

Digestion Notes (Biology 12) I. Introduction/Overview • Digestion: Breakdown of food into small, soluble molecules • Occurs physically and chemically • Absorption: The process of taking specific compounds into the body • Elimination: Expulsion of materials not absorbed into the body • Excretion: Removal of waste from metabolic processes II. Location of Parts and Function A. Teeth • Type of teeth depends on diet: • Carnivores: Sharp teeth for grasping prey and severing meat • Herbivores: Flat teeth for crushing plant fibers • Omnivores: A combination of tooth types for eating both meat and plants • Structure: • Enamel: Hard outer layer • Dentin: Bony layer under enamel • Pulp: Living part of the tooth (contains nerves and blood vessels) • Teeth are embedded in sockets in the jaw B. Tongue • Functions: • Taste: Detects salt, sour, sweet, and bitter flavors • Positioning food for chewing C. Salivary Glands • Three pairs: • Parotid (side of face; swells with mumps) • Sublingual (under tongue) • Submandibular (lower jaw) • Produce saliva, which contains enzymes for digestion D. Palates • Located at the top of the mouth • Hard palate: Front, separates the mouth from the nasal cavity • Soft palate: Back, ends in the uvula E. Pharynx • Area between mouth and esophagus • Used for both breathing and eating • Epiglottis: Closes over the glottis when swallowing to prevent choking F. Esophagus • Muscular tube that pushes food into the stomach using peristalsis • Composed of five tissue layers: 1. Mucosa (epithelial lining) 2. Submucosa (connective tissue) 3. Muscularis (two muscle layers: circular and longitudinal) 4. Serosa (outer epithelial layer; secretes fluid for lubrication) G. Cardiac Sphincter • Muscle at the junction of the esophagus and stomach • Opens to allow food into the stomach H. Stomach • J-shaped organ, located left of the body’s center • Capacity: About 1 liter • Inner lining contains gastric glands: • Parietal cells → Produce HCl • Chief cells → Produce pepsinogen, activated by HCl into pepsin • Epithelial cells → Produce mucus (protects stomach lining) • Functions: • Storage of food (empties in 2-6 hours) • Digestion using pepsin and salivary amylase • Absorption of water, ethanol • Regulation of pepsin production by the hormone gastrin I. Pyloric Sphincter • Muscle at the junction of the stomach and small intestine • Opens to allow chyme (partially digested food) into the small intestine J. Small Intestine • Length: ~ 3 meters (10 feet) • Highly convoluted to increase surface area for absorption • Interior folds covered with villi (tiny projections that increase surface area) • Divided into three parts: 1. Duodenum (first 25 cm): Produces lactase, peptidase, maltase, nuclease 2. Jejunum 3. Ileum • Functions: • Completes digestion • Absorbs nutrients into the bloodstream K. Liver • Largest organ in the body • Monitors blood composition via the hepatic portal vein L. Pancreas • Produces pancreatic juice (digestive enzymes and sodium bicarbonate to neutralize stomach acid) • Produces insulin (regulates blood glucose) M. Ileo-Caecal Opening • Joins the small intestine to the large intestine N. Caecum • Blind pouch at the end of the small intestine • No function in humans (vestigial), but in herbivores, it helps digest cellulose O. Large Intestine • Parts: 1. Ascending colon 2. Transverse colon 3. Descending colon 4. Rectum (stores feces) 5. Anus (controls feces release) • Functions: • Reabsorbs water (~95% of 10L daily intake) • Forms feces • Produces vitamins B and K using E. coli bacteria III. Digestive Enzymes Enzyme Source pH Digested Food Product Salivary Amylase Salivary Glands 7 Starch Maltose Pepsin Stomach 2 Protein Peptides Pancreatic Amylase Pancreas Basic Starch Maltose Trypsin Pancreas Basic Protein Peptides Lipase Pancreas Basic Fat Glycerol & Fatty Acids Peptidases Small Intestine Basic Peptides Amino Acids Maltase Small Intestine Basic Maltose Glucose Nuclease Pancreas Basic DNA/RNA Nucleotides IV. Swallowing and Peristalsis • Swallowing: Food forms a bolus (food ball) and is moved down the esophagus • Peristalsis: Rhythmic contractions of smooth muscle that push food through the digestive tract V. The 7 Functions of the Liver 1. Detoxifies harmful substances (e.g., alcohol) 2. Stores glucose as glycogen 3. Destroys old red blood cells (recycling heme into bile) 4. Produces urea from amino acid breakdown 5. Makes blood proteins 6. Stores iron and vitamins A, D, E, K 7. Converts amino acids to glucose if needed (gluconeogenesis) VI. Digestive Juices & Hormones Gastric Juice (Stomach) • Contains HCl, pepsinogen (activated into pepsin), and mucus • Helps digest proteins into peptides Pancreatic Juice • Contains sodium bicarbonate (neutralizes acid) • Enzymes: Pancreatic amylase, trypsin, lipase, nuclease Bile (Liver & Gallbladder) • Breaks down fats into small droplets for lipase to act on VII. Control of Digestive Gland Secretions • Nervous Reflex: Presence of food triggers digestion • Conditioned Reflex: External stimuli (e.g

Glycerol feeder sugar

Chapter 9 – Skeletal Muscles 1. Connective Tissue Surrounding a Skeletal Muscle: • Epimysium: Surrounds the entire muscle. • Perimysium: Surrounds bundles of muscle fibers (fascicles). • Endomysium: Surrounds individual muscle fibers. 2. Histology and Function of Sarcomeres: • Histology: Sarcomeres are the structural and functional units of skeletal muscles, composed of repeating units between two Z-lines. • Function: They enable muscle contraction through the sliding filament mechanism. 3. Main Components: • Thin Filaments: Actin, tropomyosin, and troponin. • Thick Filaments: Myosin. 4. Function of Transverse Tubules and Sarcoplasmic Reticulum: • Transverse Tubules (T-tubules): Transmit action potentials deep into the muscle fiber. • Sarcoplasmic Reticulum: Stores and releases calcium ions for muscle contraction. 5. Motor Unit: A motor neuron and all the muscle fibers it innervates. 6. Neuromuscular Junction: The synapse where a motor neuron meets a muscle fiber, allowing for signal transmission. 7. Synapse: A junction between two neurons or a neuron and a muscle cell where communication occurs. 8. Actions of Acetylcholine (ACh): • Initiates muscle contraction by binding to receptors on the sarcolemma. • Degraded by: Acetylcholinesterase. 9. Neurotransmitter Released at Motor Axon Terminals: Acetylcholine. 10. Steps in Excitation-Contraction Coupling: • Action potential travels along sarcolemma. • Calcium is released from the sarcoplasmic reticulum. • Calcium binds to troponin, causing tropomyosin to move, exposing binding sites on actin. • Myosin heads form cross-bridges and initiate contraction. 11. Order of Muscle Fiber Contraction: • Action potential → Calcium release → Cross-bridge formation → Power stroke → ATP binding → Cross-bridge detachment. 12. Mechanism of Muscle Contraction: • Sliding filament theory: Actin and myosin filaments slide past each other. 13. Interaction of Actin, Myosin, and Calcium: • Calcium binds to troponin, shifting tropomyosin to expose myosin-binding sites on actin, enabling cross-bridge cycling. 14. Cross-Bridges: Myosin heads that bind to actin during contraction. 15. Contraction Types: • Isotonic: Muscle length changes. • Eccentric: Muscle lengthens under tension. • Isometric: Muscle tension without length change. • Concentric: Muscle shortens under tension. 16. Force of Muscle Contraction: • Controlled by motor unit recruitment. • Partial Tetany: Incomplete relaxation. • Fused Tetany: Sustained contraction without relaxation. 17. Bones and Muscles as Levers: • Fulcrum: Pivot point of the lever. 18. Synergist and Antagonist: • Synergist: Assists the primary mover. • Antagonist: Opposes the primary mover. 19. Muscle Atrophy: Wasting of muscle due to disuse or disease. 20. Myasthenia Gravis: Autoimmune disorder causing muscle weakness by targeting ACh receptors. 21. Linea Alba: A fibrous structure running down the midline of the abdomen. 22. Origin, Insertion, and Actions of Specific Muscles: (Let me know which specific ones you’d like to focus on.) Chapter 17 – Digestive System 1. Alimentary Canal: A continuous muscular tube extending from the mouth to the anus. 2. Functions of the Digestive System: • Ingestion, digestion, absorption, and elimination. 3. Breakdown and Absorption: • Carbohydrates: Begin in the mouth (amylase). • Proteins: Start in the stomach (pepsin). • Fats: Start in the small intestine (lipase, bile). 4. Layers of Alimentary Canal Walls: • Mucosa, submucosa, muscularis, serosa. 5. Accessory Organs: • Liver, pancreas, gallbladder. 6. Sympathetic vs. Parasympathetic Effects: • Sympathetic: Decreases digestion. • Parasympathetic: Enhances digestion. 7. Hormones: • Gastrin: Stimulates gastric juice secretion. • Cholecystokinin (CCK): Stimulates bile and pancreatic juice. • Secretin: Stimulates bicarbonate secretion. 8. Peristalsis vs. Segmentation: • Peristalsis: Wave-like contractions. • Segmentation: Mixing movements. 9. Epiglottis Function: Prevents food from entering the trachea. 10. Heartburn: Caused by stomach acid reflux into the esophagus. 11. Stomach Parts: Fundus, body, pylorus. 12. Secretions: • Parietal Cells: Hydrochloric acid, intrinsic factor. • Chief Cells: Pepsinogen. 13. Digestive Enzymes and Substances: • Amylase: Breaks down starch. • Pepsin: Digests proteins. • Trypsin: Protein digestion. • Lipase: Fat digestion. • Bile Salts: Emulsify fats. 14. Liver, Gallbladder, Pancreas Functions: • Liver: Produces bile. • Gallbladder: Stores bile. • Pancreas: Produces enzymes and bicarbonate. 15. Anatomy of Bile Ducts: • Common hepatic, cystic, and pancreatic ducts form the common bile duct. 16. Functions of Large Intestine: • Absorption of water, vitamin production, and feces formation. 17. Defecation Reflex: Triggered by rectal wall distension. Chapter 18 – Nutrition 1. Excess Glucose Storage: As glycogen in the liver and muscles. 2. Tissue Requiring Glucose: Nervous tissue (brain). 3. Triglyceride Components: Glycerol and three fatty acids. 4. Essential Amino Acids: Cannot be synthesized by the body

Chapter Summary 2.1 The Importance of Chemistry in Anatomy and Physiology Chemicals are all around us. Household products such as soap and shampoo as well as food and medicine are comprised of chemicals. The human body is also made of chemicals. We begin our examination of anatomy and physiology with a study of basic chemistry. 2.2 Fundamentals of Chemistry Matter is anything that has mass and takes up space. 1. Elements and atoms a. Naturally occurring matter on Earth is composed of ninety-two elements. b. Elements usually combine to form compounds. c. Elements are composed of atoms. d. Atoms of different elements vary in size, weight, and ways of interacting. 2. Atomic structure a. An atom consists of electrons surrounding a nucleus, which has protons and neutrons. The exception is hydrogen, which has only a proton in its nucleus. b. Electrons are negatively charged, protons positively charged, and neutrons uncharged. c. A complete atom is electrically neutral. d. The atomic number of an element is equal to the number of protons in each atom. 3. Isotopes a. Isotopes are atoms with the same atomic number but different mass numbers (due to differing numbers of neutrons). The atomic weight of an element is the average of the mass numbers of its various isotopes. b. All the isotopes of an element react chemically in the same manner. c. Some isotopes are radioactive and release atomic radiation. 4. Molecules and compounds a. Two or more atoms may combine to form a molecule. b. A molecular formula represents the numbers and types of atoms in a molecule. c. If atoms of the same element combine, they produce molecules of that element. d. If atoms of different elements combine, they form molecules called compounds. 2.3 Bonding of Atoms When atoms form links called bonds, they gain, lose, or share electrons. Electrons occupy space in areas called electron shells that encircle an atomic nucleus. Atoms with completely filled outer shells are inert, whereas atoms with incompletely filled outer shells gain, lose, or share electrons and thus become stable. 1. Ionic bonds a. Atoms that lose electrons become positively charged (cations); atoms that gain electrons become negatively charged (anions). b. Ions with opposite charges attract and join by ionic bonds. 2. Atoms that share electrons join by covalent bonds. a. Nonpolar molecules result from an equal sharing of electrons. b. Polar molecules result from an unequal sharing of electrons. c. Hydrogen bonds may form within and between polar molecules. 3. Chemical reactions a. In a chemical reaction, bonds between atoms, ions, or molecules break or form. Starting materials are called reactants; the resulting atoms or molecules are called products. b. Three types of chemical reactions are synthesis, in which large molecules build up from smaller ones; decomposition, in which molecules break down; and exchange reactions, in which parts of two different molecules trade positions. c. Many reactions are reversible. The direction of a reaction depends upon the proportion of reactants and products and the energy available. d. Catalysts (enzymes) influence the rate (not the direction) of the reaction. 2.4 Electrolytes, Acids and Bases, and Salts Compounds that ionize in water are electrolytes. 1. Electrolytes that release hydrogen ions are acids, and those that release hydroxide or other ions that react with hydrogen ions are bases. a. Acids and bases react to form water and electrolytes called salts. 2. Acid and base concentrations a. pH represents the concentration of hydrogen ions (H+) and hydroxide ions (OH−) in a solution. b. A solution with equal numbers of H+ and OH− is neutral and has a pH of 7.0; a solution with more H+ than OH− is acidic (pH less than 7.0); a solution with fewer H+ than OH− is basic (pH greater than 7.0). c. A tenfold difference in hydrogen ion concentration separates each whole number in the pH scale. d. Buffers are chemicals that resist pH change. 2.5 Chemical Constituents of Cells Molecules containing carbon and hydrogen atoms are organic and are usually nonelectrolytes; other molecules are inorganic and are usually electrolytes. 1. Inorganic substances a. Water is the most abundant compound in the body. Many chemical reactions take place in water. Water transports chemicals and heat and helps release excess body heat. b. Oxygen releases energy for metabolic activities from glucose and other molecules. c. Carbon dioxide is produced when certain metabolic processes release energy. d. Inorganic salts provide ions needed in a variety of metabolic processes. e. Electrolytes must be present in certain concentrations inside and outside of cells. 2. Organic substances a. Carbohydrates provide much of the energy cells require and are built of simple sugar molecules. b. Lipids, such as triglycerides (fats), phospholipids, and steroids, supply energy and are used to build cell parts. 1) The building blocks of triglycerides are glycerol and three fatty acids. 2) The building blocks of phospholipids are glycerol, two fatty acids, and a phosphate group. 3) Steroids include rings of carbon atoms and are synthesized in the body from cholesterol. c. Proteins serve as structural materials, energy sources, hormones, cell surface receptors, antibodies, and enzymes that speed chemical reactions without being consumed. 1) The building blocks of proteins are amino acids. 2) Proteins vary in the numbers and types of their constituent amino acids; the sequences of these amino acids; and their three-dimensional structures, or conformations. 3) Primary structure is the amino acid sequence. Secondary structure comes from attractions between amino acids that are close together in the primary structure. Tertiary structure reflects attractions of far-apart amino acids and folds the molecule. The amino acid sequence determines the protein’s conformation. 4) The protein’s conformation determines its function. 5) Exposure to excessive heat, radiation, electricity, or certain chemicals can denature proteins. d. Nucleic acids constitute genes, the instructions that control cell activities, and direct protein synthesis. 1) The two types are RNA and DNA. 2) Nucleic acid building blocks are nucleotides. 3) DNA molecules store information that cell parts use to construct specific proteins. 4) RNA molecules help synthesize proteins. 5) DNA molecules are replicated, and an exact copy of the original cell’s DNA is passed to each of the newly formed cells resulting from cell division.

lecture 27: synthesis of Triacyl glycerols and major membrane lipids

β-oxidation and glycerol catabolism

NurBio Lec - Glycerol Catabolism / B-Oxidation / Amino Acid Metabolism / Vitamins and Minerals

Chapter 6- Lipids, Membranes, and the First Cells

4 main classes of macromolecules carbohydrates, proteins, lipids, nucleic acids whats the difference between polymers and monomers? a monomer is 1 building block, a polymer is many monomers what is the reactant of dehydration synthesis? product? reactant is 2 or more monomers, the product is a polymer what is the reactant of hydrolysis? product? reactant is a polymer, the product are monomers Common name for Carbohydrates? glucose monomers of carbohydrates monosaccharides What type of bonds do monosaccharides form? glycosidic linkage What do we call two monomers joined together by one of these bonds? polysaccharide How are polysaccharides used in the body? either as building blocks or energy reserves What polysaccharide is used by plants? What is it composed of? Glucose, entirely of glucose monomers What polysaccharide is used by animals? What is it composed of? Glycogen, highly branched glucose Differentiate between alpha and beta linkages. alpha has OH below, beta has OH above What type of carbohydrates have alpha/beta linkages? glucose monomers, cellulose, and starch What qualities do starch gain from its alpha linkages? makes a helix shape and lets it connect What qualities do cellulose gain from its beta linkages? Makes a linear shape What is chitin? Where is it found? Structural polysaccharide found in cell wall of fungi and arthropods. What type of linkages does chitin have? beta linkages . Why don't lipids have an affinity for water? non-polar Describe the composition of a fat. they are made up of glycerol and fatty acids What is the composition of a triglyceride? a glycerol bound to 3 fatty acids How is a triglyceride formed? What type of bonds? 3 fatty acids joined to a glycerol by dehydration synthesis saturated fatty acids Saturated had hydrogen bonds at every position and no carbon carbon bonds Unsaturated fatty acids unsaturated has carbon- carbon bonds and have a kink in the skeleton What property of unsaturated acids makes them liquid at room temperature? they are bent Do saturated or unsaturated fatty acids have a lower melting point? saturated What is the main function of fats? What makes them so good at this? they store twice the amount of energy that carbohydrate do Describe the structure and function of a phospholipid. glycerol connected to 2 fatty acids and a phosphate, forms the cell wall What part of the phospholipid is hydrophobic? tails What part of a phospholipid is hydrophilic? head Describe the arrangement of phospholipids in a membrane. Why do phospholipids arrange themselves in such a way? They make a bilayer, tail avoid water inside Describe the structure of a steroid. 4 fused carbon rings What are some examples of steroids? cholesterol, estrogen, testosterone What are some functions of proteins? structure, support, storage, transport, defense, movement What are the monomers of proteins? amino acids What 4 things are attached to the central carbon of the amino acid? hydrogen atom, carboxyl group, amino group, R variable What is the significance of the R group? determine the characteristics of an amino acids How are amino acids joined? dehydration synthesis What type of bond is formed between the amino acids? peptide bonds What are the names of the two ends of the polypeptide chain of amino acids? n and c terminals How do the two ends of the polypeptide chain get their names? n has a free amino group, c has a free carboxyl group How do proteins form from a polypeptide chain? interactions in the polypeptide make the polypeptide chain and different amino acids form What type of bond is formed in a polypeptide chain? peptide bond Define primary structure. order of amino acids Define secondary structure. What holds it together? coiled and folded shaped bond, hydrogen bonds Describe an alpha helix. What holds it together? a coil, every 4th amino acid has a hydrogen bond Describe a beta pleated sheet. What holds it together? a folding shape, hydrogen bonds hold it in the parallel peptide backbones Describe tertiary structure. 3d shape of a protein determined by the r group How to sulfhydryl groups contribute to the tertiary structure of a protein? strong covalent bonds/disulfide bridges How does quaternary structure arise? aggregation of 2 or more polypeptides How is quaternary different from tertiary? has 4 different polypeptides What factors can lead to the denaturation of proteins? physical and chemical condition of its environment How might this affect the function of the protein? it becomes biologically inactive What is the function of chaperonins? they help fold proteins What might happen if chaperonins don't function properly? it can lead to diseases What are the two types of nucleic acids? DNA and RNA What are nucleic acids monomers? nucleotides Describe the path that information taken from DNA to protein. DNA Gives information to RNA, RNA makes proteins Describe the makeup of a nucleotide. a nitrogenous base, pentose sugar, phosphate group What are the four bases of DNA? Adenine, Thymine, Cytosine, Guanine Distinguish between purines and pyrimidines. Purines have 1 6 ringed side and one 5 ringed side, Pyrimidines have 1 ring with 6 sides Which bases are purines and which are pyrimidines? Purines: Adenine and Guanine Pyrimidines: Thymine and Cytosine sugar pentose for rna? ribose sugar pentose for DNA? deoxyribose does not have oxygen on carbon 2 What type of bonds are formed between nucleotides? Where on the nucleotide are these bonds formed? phosphodiester bonds, the OH 3 end connects to the phosphate 5 end Describe the double helix of DNA. What's on the inside? What's on the outside? sugar phosphate backbone outside, nitrogenous bases inside What holds the double helix of DNA together? hydrogen bonds How does the cell ensure the DNA will copy correctly? each strand acts likea template What distinguishes RNA from DNA? uracil and single stranded

4 main classes of macromolecules carbohydrates, proteins, lipids, nucleic acids whats the difference between polymers and monomers? a monomer is 1 building block, a polymer is many monomers what is the reactant of dehydration synthesis? product? reactant is 2 or more monomers, the product is a polymer what is the reactant of hydrolysis? product? reactant is a polymer, the product are monomers Common name for Carbohydrates? glucose monomers of carbohydrates monosaccharides What type of bonds do monosaccharides form? glycosidic linkage What do we call two monomers joined together by one of these bonds? polysaccharide How are polysaccharides used in the body? either as building blocks or energy reserves What polysaccharide is used by plants? What is it composed of? Glucose, entirely of glucose monomers What polysaccharide is used by animals? What is it composed of? Glycogen, highly branched glucose Differentiate between alpha and beta linkages. alpha has OH below, beta has OH above What type of carbohydrates have alpha/beta linkages? glucose monomers, cellulose, and starch What qualities do starch gain from its alpha linkages? makes a helix shape and lets it connect What qualities do cellulose gain from its beta linkages? Makes a linear shape What is chitin? Where is it found? Structural polysaccharide found in cell wall of fungi and arthropods. What type of linkages does chitin have? beta linkages . Why don't lipids have an affinity for water? non-polar Describe the composition of a fat. they are made up of glycerol and fatty acids What is the composition of a triglyceride? a glycerol bound to 3 fatty acids How is a triglyceride formed? What type of bonds? 3 fatty acids joined to a glycerol by dehydration synthesis saturated fatty acids Saturated had hydrogen bonds at every position and no carbon carbon bonds Unsaturated fatty acids unsaturated has carbon- carbon bonds and have a kink in the skeleton What property of unsaturated acids makes them liquid at room temperature? they are bent Do saturated or unsaturated fatty acids have a lower melting point? saturated What is the main function of fats? What makes them so good at this? they store twice the amount of energy that carbohydrate do Describe the structure and function of a phospholipid. glycerol connected to 2 fatty acids and a phosphate, forms the cell wall What part of the phospholipid is hydrophobic? tails What part of a phospholipid is hydrophilic? head Describe the arrangement of phospholipids in a membrane. Why do phospholipids arrange themselves in such a way? They make a bilayer, tail avoid water inside Describe the structure of a steroid. 4 fused carbon rings What are some examples of steroids? cholesterol, estrogen, testosterone What are some functions of proteins? structure, support, storage, transport, defense, movement What are the monomers of proteins? amino acids What 4 things are attached to the central carbon of the amino acid? hydrogen atom, carboxyl group, amino group, R variable What is the significance of the R group? determine the characteristics of an amino acids How are amino acids joined? dehydration synthesis What type of bond is formed between the amino acids? peptide bonds What are the names of the two ends of the polypeptide chain of amino acids? n and c terminals How do the two ends of the polypeptide chain get their names? n has a free amino group, c has a free carboxyl group How do proteins form from a polypeptide chain? interactions in the polypeptide make the polypeptide chain and different amino acids form What type of bond is formed in a polypeptide chain? peptide bond Define primary structure. order of amino acids Define secondary structure. What holds it together? coiled and folded shaped bond, hydrogen bonds Describe an alpha helix. What holds it together? a coil, every 4th amino acid has a hydrogen bond Describe a beta pleated sheet. What holds it together? a folding shape, hydrogen bonds hold it in the parallel peptide backbones Describe tertiary structure. 3d shape of a protein determined by the r group How to sulfhydryl groups contribute to the tertiary structure of a protein? strong covalent bonds/disulfide bridges How does quaternary structure arise? aggregation of 2 or more polypeptides How is quaternary different from tertiary? has 4 different polypeptides What factors can lead to the denaturation of proteins? physical and chemical condition of its environment How might this affect the function of the protein? it becomes biologically inactive What is the function of chaperonins? they help fold proteins What might happen if chaperonins don't function properly? it can lead to diseases What are the two types of nucleic acids? DNA and RNA What are nucleic acids monomers? nucleotides Describe the path that information taken from DNA to protein. DNA Gives information to RNA, RNA makes proteins Describe the makeup of a nucleotide. a nitrogenous base, pentose sugar, phosphate group What are the four bases of DNA? Adenine, Thymine, Cytosine, Guanine Distinguish between purines and pyrimidines. Purines have 1 6 ringed side and one 5 ringed side, Pyrimidines have 1 ring with 6 sides Which bases are purines and which are pyrimidines? Purines: Adenine and Guanine Pyrimidines: Thymine and Cytosine sugar pentose for rna? ribose sugar pentose for DNA? deoxyribose does not have oxygen on carbon 2 What type of bonds are formed between nucleotides? Where on the nucleotide are these bonds formed? phosphodiester bonds, the OH 3 end connects to the phosphate 5 end Describe the double helix of DNA. What's on the inside? What's on the outside? sugar phosphate backbone outside, nitrogenous bases inside What holds the double helix of DNA together? hydrogen bonds How does the cell ensure the DNA will copy correctly? each strand acts likea template What distinguishes RNA from DNA? uracil and single stranded

4 main classes of macromolecules carbohydrates, proteins, lipids, nucleic acids whats the difference between polymers and monomers? a monomer is 1 building block, a polymer is many monomers what is the reactant of dehydration synthesis? product? reactant is 2 or more monomers, the product is a polymer what is the reactant of hydrolysis? product? reactant is a polymer, the product are monomers Common name for Carbohydrates? glucose monomers of carbohydrates monosaccharides What type of bonds do monosaccharides form? glycosidic linkage What do we call two monomers joined together by one of these bonds? polysaccharide How are polysaccharides used in the body? either as building blocks or energy reserves What polysaccharide is used by plants? What is it composed of? Glucose, entirely of glucose monomers What polysaccharide is used by animals? What is it composed of? Glycogen, highly branched glucose Differentiate between alpha and beta linkages. alpha has OH below, beta has OH above What type of carbohydrates have alpha/beta linkages? glucose monomers, cellulose, and starch What qualities do starch gain from its alpha linkages? makes a helix shape and lets it connect What qualities do cellulose gain from its beta linkages? Makes a linear shape What is chitin? Where is it found? Structural polysaccharide found in cell wall of fungi and arthropods. What type of linkages does chitin have? beta linkages . Why don't lipids have an affinity for water? non-polar Describe the composition of a fat. they are made up of glycerol and fatty acids What is the composition of a triglyceride? a glycerol bound to 3 fatty acids How is a triglyceride formed? What type of bonds? 3 fatty acids joined to a glycerol by dehydration synthesis saturated fatty acids Saturated had hydrogen bonds at every position and no carbon carbon bonds Unsaturated fatty acids unsaturated has carbon- carbon bonds and have a kink in the skeleton What property of unsaturated acids makes them liquid at room temperature? they are bent Do saturated or unsaturated fatty acids have a lower melting point? saturated What is the main function of fats? What makes them so good at this? they store twice the amount of energy that carbohydrate do Describe the structure and function of a phospholipid. glycerol connected to 2 fatty acids and a phosphate, forms the cell wall What part of the phospholipid is hydrophobic? tails What part of a phospholipid is hydrophilic? head Describe the arrangement of phospholipids in a membrane. Why do phospholipids arrange themselves in such a way? They make a bilayer, tail avoid water inside Describe the structure of a steroid. 4 fused carbon rings What are some examples of steroids? cholesterol, estrogen, testosterone What are some functions of proteins? structure, support, storage, transport, defense, movement What are the monomers of proteins? amino acids What 4 things are attached to the central carbon of the amino acid? hydrogen atom, carboxyl group, amino group, R variable What is the significance of the R group? determine the characteristics of an amino acids How are amino acids joined? dehydration synthesis What type of bond is formed between the amino acids? peptide bonds What are the names of the two ends of the polypeptide chain of amino acids? n and c terminals How do the two ends of the polypeptide chain get their names? n has a free amino group, c has a free carboxyl group How do proteins form from a polypeptide chain? interactions in the polypeptide make the polypeptide chain and different amino acids form What type of bond is formed in a polypeptide chain? peptide bond Define primary structure. order of amino acids Define secondary structure. What holds it together? coiled and folded shaped bond, hydrogen bonds Describe an alpha helix. What holds it together? a coil, every 4th amino acid has a hydrogen bond Describe a beta pleated sheet. What holds it together? a folding shape, hydrogen bonds hold it in the parallel peptide backbones Describe tertiary structure. 3d shape of a protein determined by the r group How to sulfhydryl groups contribute to the tertiary structure of a protein? strong covalent bonds/disulfide bridges How does quaternary structure arise? aggregation of 2 or more polypeptides How is quaternary different from tertiary? has 4 different polypeptides What factors can lead to the denaturation of proteins? physical and chemical condition of its environment How might this affect the function of the protein? it becomes biologically inactive What is the function of chaperonins? they help fold proteins What might happen if chaperonins don't function properly? it can lead to diseases What are the two types of nucleic acids? DNA and RNA What are nucleic acids monomers? nucleotides Describe the path that information taken from DNA to protein. DNA Gives information to RNA, RNA makes proteins Describe the makeup of a nucleotide. a nitrogenous base, pentose sugar, phosphate group What are the four bases of DNA? Adenine, Thymine, Cytosine, Guanine Distinguish between purines and pyrimidines. Purines have 1 6 ringed side and one 5 ringed side, Pyrimidines have 1 ring with 6 sides Which bases are purines and which are pyrimidines? Purines: Adenine and Guanine Pyrimidines: Thymine and Cytosine sugar pentose for rna? ribose sugar pentose for DNA? deoxyribose does not have oxygen on carbon 2 What type of bonds are formed between nucleotides? Where on the nucleotide are these bonds formed? phosphodiester bonds, the OH 3 end connects to the phosphate 5 end Describe the double helix of DNA. What's on the inside? What's on the outside? sugar phosphate backbone outside, nitrogenous bases inside What holds the double helix of DNA together? hydrogen bonds How does the cell ensure the DNA will copy correctly? each strand acts likea template What distinguishes RNA from DNA? uracil and single stranded

4 main classes of macromolecules carbohydrates, proteins, lipids, nucleic acids whats the difference between polymers and monomers? a monomer is 1 building block, a polymer is many monomers what is the reactant of dehydration synthesis? product? reactant is 2 or more monomers, the product is a polymer what is the reactant of hydrolysis? product? reactant is a polymer, the product are monomers Common name for Carbohydrates? glucose monomers of carbohydrates monosaccharides What type of bonds do monosaccharides form? glycosidic linkage What do we call two monomers joined together by one of these bonds? polysaccharide How are polysaccharides used in the body? either as building blocks or energy reserves What polysaccharide is used by plants? What is it composed of? Glucose, entirely of glucose monomers What polysaccharide is used by animals? What is it composed of? Glycogen, highly branched glucose Differentiate between alpha and beta linkages. alpha has OH below, beta has OH above What type of carbohydrates have alpha/beta linkages? glucose monomers, cellulose, and starch What qualities do starch gain from its alpha linkages? makes a helix shape and lets it connect What qualities do cellulose gain from its beta linkages? Makes a linear shape What is chitin? Where is it found? Structural polysaccharide found in cell wall of fungi and arthropods. What type of linkages does chitin have? beta linkages . Why don't lipids have an affinity for water? non-polar Describe the composition of a fat. they are made up of glycerol and fatty acids What is the composition of a triglyceride? a glycerol bound to 3 fatty acids How is a triglyceride formed? What type of bonds? 3 fatty acids joined to a glycerol by dehydration synthesis saturated fatty acids Saturated had hydrogen bonds at every position and no carbon carbon bonds Unsaturated fatty acids unsaturated has carbon- carbon bonds and have a kink in the skeleton What property of unsaturated acids makes them liquid at room temperature? they are bent Do saturated or unsaturated fatty acids have a lower melting point? saturated What is the main function of fats? What makes them so good at this? they store twice the amount of energy that carbohydrate do Describe the structure and function of a phospholipid. glycerol connected to 2 fatty acids and a phosphate, forms the cell wall What part of the phospholipid is hydrophobic? tails What part of a phospholipid is hydrophilic? head Describe the arrangement of phospholipids in a membrane. Why do phospholipids arrange themselves in such a way? They make a bilayer, tail avoid water inside Describe the structure of a steroid. 4 fused carbon rings What are some examples of steroids? cholesterol, estrogen, testosterone What are some functions of proteins? structure, support, storage, transport, defense, movement What are the monomers of proteins? amino acids What 4 things are attached to the central carbon of the amino acid? hydrogen atom, carboxyl group, amino group, R variable What is the significance of the R group? determine the characteristics of an amino acids How are amino acids joined? dehydration synthesis What type of bond is formed between the amino acids? peptide bonds What are the names of the two ends of the polypeptide chain of amino acids? n and c terminals How do the two ends of the polypeptide chain get their names? n has a free amino group, c has a free carboxyl group How do proteins form from a polypeptide chain? interactions in the polypeptide make the polypeptide chain and different amino acids form What type of bond is formed in a polypeptide chain? peptide bond Define primary structure. order of amino acids Define secondary structure. What holds it together? coiled and folded shaped bond, hydrogen bonds Describe an alpha helix. What holds it together? a coil, every 4th amino acid has a hydrogen bond Describe a beta pleated sheet. What holds it together? a folding shape, hydrogen bonds hold it in the parallel peptide backbones Describe tertiary structure. 3d shape of a protein determined by the r group How to sulfhydryl groups contribute to the tertiary structure of a protein? strong covalent bonds/disulfide bridges How does quaternary structure arise? aggregation of 2 or more polypeptides How is quaternary different from tertiary? has 4 different polypeptides What factors can lead to the denaturation of proteins? physical and chemical condition of its environment How might this affect the function of the protein? it becomes biologically inactive What is the function of chaperonins? they help fold proteins What might happen if chaperonins don't function properly? it can lead to diseases What are the two types of nucleic acids? DNA and RNA What are nucleic acids monomers? nucleotides Describe the path that information taken from DNA to protein. DNA Gives information to RNA, RNA makes proteins Describe the makeup of a nucleotide. a nitrogenous base, pentose sugar, phosphate group What are the four bases of DNA? Adenine, Thymine, Cytosine, Guanine Distinguish between purines and pyrimidines. Purines have 1 6 ringed side and one 5 ringed side, Pyrimidines have 1 ring with 6 sides Which bases are purines and which are pyrimidines? Purines: Adenine and Guanine Pyrimidines: Thymine and Cytosine sugar pentose for rna? ribose sugar pentose for DNA? deoxyribose does not have oxygen on carbon 2 What type of bonds are formed between nucleotides? Where on the nucleotide are these bonds formed? phosphodiester bonds, the OH 3 end connects to the phosphate 5 end Describe the double helix of DNA. What's on the inside? What's on the outside? sugar phosphate backbone outside, nitrogenous bases inside What holds the double helix of DNA together? hydrogen bonds How does the cell ensure the DNA will copy correctly? each strand acts likea template What distinguishes RNA from DNA? uracil and single stranded

4 main classes of macromolecules carbohydrates, proteins, lipids, nucleic acids whats the difference between polymers and monomers? a monomer is 1 building block, a polymer is many monomers what is the reactant of dehydration synthesis? product? reactant is 2 or more monomers, the product is a polymer what is the reactant of hydrolysis? product? reactant is a polymer, the product are monomers Common name for Carbohydrates? glucose monomers of carbohydrates monosaccharides What type of bonds do monosaccharides form? glycosidic linkage What do we call two monomers joined together by one of these bonds? polysaccharide How are polysaccharides used in the body? either as building blocks or energy reserves What polysaccharide is used by plants? What is it composed of? Glucose, entirely of glucose monomers What polysaccharide is used by animals? What is it composed of? Glycogen, highly branched glucose Differentiate between alpha and beta linkages. alpha has OH below, beta has OH above What type of carbohydrates have alpha/beta linkages? glucose monomers, cellulose, and starch What qualities do starch gain from its alpha linkages? makes a helix shape and lets it connect What qualities do cellulose gain from its beta linkages? Makes a linear shape What is chitin? Where is it found? Structural polysaccharide found in cell wall of fungi and arthropods. What type of linkages does chitin have? beta linkages . Why don't lipids have an affinity for water? non-polar Describe the composition of a fat. they are made up of glycerol and fatty acids What is the composition of a triglyceride? a glycerol bound to 3 fatty acids How is a triglyceride formed? What type of bonds? 3 fatty acids joined to a glycerol by dehydration synthesis saturated fatty acids Saturated had hydrogen bonds at every position and no carbon carbon bonds Unsaturated fatty acids unsaturated has carbon- carbon bonds and have a kink in the skeleton What property of unsaturated acids makes them liquid at room temperature? they are bent Do saturated or unsaturated fatty acids have a lower melting point? saturated What is the main function of fats? What makes them so good at this? they store twice the amount of energy that carbohydrate do Describe the structure and function of a phospholipid. glycerol connected to 2 fatty acids and a phosphate, forms the cell wall What part of the phospholipid is hydrophobic? tails What part of a phospholipid is hydrophilic? head Describe the arrangement of phospholipids in a membrane. Why do phospholipids arrange themselves in such a way? They make a bilayer, tail avoid water inside Describe the structure of a steroid. 4 fused carbon rings What are some examples of steroids? cholesterol, estrogen, testosterone What are some functions of proteins? structure, support, storage, transport, defense, movement What are the monomers of proteins? amino acids What 4 things are attached to the central carbon of the amino acid? hydrogen atom, carboxyl group, amino group, R variable What is the significance of the R group? determine the characteristics of an amino acids How are amino acids joined? dehydration synthesis What type of bond is formed between the amino acids? peptide bonds What are the names of the two ends of the polypeptide chain of amino acids? n and c terminals How do the two ends of the polypeptide chain get their names? n has a free amino group, c has a free carboxyl group How do proteins form from a polypeptide chain? interactions in the polypeptide make the polypeptide chain and different amino acids form What type of bond is formed in a polypeptide chain? peptide bond Define primary structure. order of amino acids Define secondary structure. What holds it together? coiled and folded shaped bond, hydrogen bonds Describe an alpha helix. What holds it together? a coil, every 4th amino acid has a hydrogen bond Describe a beta pleated sheet. What holds it together? a folding shape, hydrogen bonds hold it in the parallel peptide backbones Describe tertiary structure. 3d shape of a protein determined by the r group How to sulfhydryl groups contribute to the tertiary structure of a protein? strong covalent bonds/disulfide bridges How does quaternary structure arise? aggregation of 2 or more polypeptides How is quaternary different from tertiary? has 4 different polypeptides What factors can lead to the denaturation of proteins? physical and chemical condition of its environment How might this affect the function of the protein? it becomes biologically inactive What is the function of chaperonins? they help fold proteins What might happen if chaperonins don't function properly? it can lead to diseases What are the two types of nucleic acids? DNA and RNA What are nucleic acids monomers? nucleotides Describe the path that information taken from DNA to protein. DNA Gives information to RNA, RNA makes proteins Describe the makeup of a nucleotide. a nitrogenous base, pentose sugar, phosphate group What are the four bases of DNA? Adenine, Thymine, Cytosine, Guanine Distinguish between purines and pyrimidines. Purines have 1 6 ringed side and one 5 ringed side, Pyrimidines have 1 ring with 6 sides Which bases are purines and which are pyrimidines? Purines: Adenine and Guanine Pyrimidines: Thymine and Cytosine sugar pentose for rna? ribose sugar pentose for DNA? deoxyribose does not have oxygen on carbon 2 What type of bonds are formed between nucleotides? Where on the nucleotide are these bonds formed? phosphodiester bonds, the OH 3 end connects to the phosphate 5 end Describe the double helix of DNA. What's on the inside? What's on the outside? sugar phosphate backbone outside, nitrogenous bases inside What holds the double helix of DNA together? hydrogen bonds How does the cell ensure the DNA will copy correctly? each strand acts likea template What distinguishes RNA from DNA? uracil and single stranded

4 main classes of macromolecules carbohydrates, proteins, lipids, nucleic acids whats the difference between polymers and monomers? a monomer is 1 building block, a polymer is many monomers what is the reactant of dehydration synthesis? product? reactant is 2 or more monomers, the product is a polymer what is the reactant of hydrolysis? product? reactant is a polymer, the product are monomers Common name for Carbohydrates? glucose monomers of carbohydrates monosaccharides What type of bonds do monosaccharides form? glycosidic linkage What do we call two monomers joined together by one of these bonds? polysaccharide How are polysaccharides used in the body? either as building blocks or energy reserves What polysaccharide is used by plants? What is it composed of? Glucose, entirely of glucose monomers What polysaccharide is used by animals? What is it composed of? Glycogen, highly branched glucose Differentiate between alpha and beta linkages. alpha has OH below, beta has OH above What type of carbohydrates have alpha/beta linkages? glucose monomers, cellulose, and starch What qualities do starch gain from its alpha linkages? makes a helix shape and lets it connect What qualities do cellulose gain from its beta linkages? Makes a linear shape What is chitin? Where is it found? Structural polysaccharide found in cell wall of fungi and arthropods. What type of linkages does chitin have? beta linkages . Why don't lipids have an affinity for water? non-polar Describe the composition of a fat. they are made up of glycerol and fatty acids What is the composition of a triglyceride? a glycerol bound to 3 fatty acids How is a triglyceride formed? What type of bonds? 3 fatty acids joined to a glycerol by dehydration synthesis saturated fatty acids Saturated had hydrogen bonds at every position and no carbon carbon bonds Unsaturated fatty acids unsaturated has carbon- carbon bonds and have a kink in the skeleton What property of unsaturated acids makes them liquid at room temperature? they are bent Do saturated or unsaturated fatty acids have a lower melting point? saturated What is the main function of fats? What makes them so good at this? they store twice the amount of energy that carbohydrate do Describe the structure and function of a phospholipid. glycerol connected to 2 fatty acids and a phosphate, forms the cell wall What part of the phospholipid is hydrophobic? tails What part of a phospholipid is hydrophilic? head Describe the arrangement of phospholipids in a membrane. Why do phospholipids arrange themselves in such a way? They make a bilayer, tail avoid water inside Describe the structure of a steroid. 4 fused carbon rings What are some examples of steroids? cholesterol, estrogen, testosterone What are some functions of proteins? structure, support, storage, transport, defense, movement What are the monomers of proteins? amino acids What 4 things are attached to the central carbon of the amino acid? hydrogen atom, carboxyl group, amino group, R variable What is the significance of the R group? determine the characteristics of an amino acids How are amino acids joined? dehydration synthesis What type of bond is formed between the amino acids? peptide bonds What are the names of the two ends of the polypeptide chain of amino acids? n and c terminals How do the two ends of the polypeptide chain get their names? n has a free amino group, c has a free carboxyl group How do proteins form from a polypeptide chain? interactions in the polypeptide make the polypeptide chain and different amino acids form What type of bond is formed in a polypeptide chain? peptide bond Define primary structure. order of amino acids Define secondary structure. What holds it together? coiled and folded shaped bond, hydrogen bonds Describe an alpha helix. What holds it together? a coil, every 4th amino acid has a hydrogen bond Describe a beta pleated sheet. What holds it together? a folding shape, hydrogen bonds hold it in the parallel peptide backbones Describe tertiary structure. 3d shape of a protein determined by the r group How to sulfhydryl groups contribute to the tertiary structure of a protein? strong covalent bonds/disulfide bridges How does quaternary structure arise? aggregation of 2 or more polypeptides How is quaternary different from tertiary? has 4 different polypeptides What factors can lead to the denaturation of proteins? physical and chemical condition of its environment How might this affect the function of the protein? it becomes biologically inactive What is the function of chaperonins? they help fold proteins What might happen if chaperonins don't function properly? it can lead to diseases What are the two types of nucleic acids? DNA and RNA What are nucleic acids monomers? nucleotides Describe the path that information taken from DNA to protein. DNA Gives information to RNA, RNA makes proteins Describe the makeup of a nucleotide. a nitrogenous base, pentose sugar, phosphate group What are the four bases of DNA? Adenine, Thymine, Cytosine, Guanine Distinguish between purines and pyrimidines. Purines have 1 6 ringed side and one 5 ringed side, Pyrimidines have 1 ring with 6 sides Which bases are purines and which are pyrimidines? Purines: Adenine and Guanine Pyrimidines: Thymine and Cytosine sugar pentose for rna? ribose sugar pentose for DNA? deoxyribose does not have oxygen on carbon 2 What type of bonds are formed between nucleotides? Where on the nucleotide are these bonds formed? phosphodiester bonds, the OH 3 end connects to the phosphate 5 end Describe the double helix of DNA. What's on the inside? What's on the outside? sugar phosphate backbone outside, nitrogenous bases inside What holds the double helix of DNA together? hydrogen bonds How does the cell ensure the DNA will copy correctly? each strand acts likea template What distinguishes RNA from DNA? uracil and single stranded