Results for "uracil"

BIOC 503 - Transcription/RNA metabolism

In eukaryotes a series of_________ residues are added to the 3' end of an RNA molecule as part of the posttranscriptional processing used to produce functional mRNA. guanine adenine cytosine uracil

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

Isotype switching & AID and uracil-DNA glycosylase activity

DNA, RNA und Proteinbiosynthese 1. DNA – Aufbau und Eigenschaften Struktur: Die DNA ist eine Doppelhelix, bestehend aus zwei antiparallelen Strängen. Jeder Strang besteht aus einer Kette von Nukleotiden. Nukleotide: Bausteine der DNA, bestehen aus: einer Desoxyribose (Zucker), einer Phosphatgruppe, einer der vier Basen: Adenin (A), Thymin (T), Guanin (G), Cytosin (C). Basenpaarung: A-T und G-C durch Wasserstoffbrückenbindungen. Antiparallelität: Die Stränge verlaufen in entgegengesetzten Richtungen (5' → 3' und 3' → 5'). Unterschied DNA vs. RNA: DNA: Doppelsträngig, enthält Desoxyribose und Thymin. RNA: Einzelsträngig, enthält Ribose und Uracil (anstatt Thymin). 2. Replikation der DNA Definition: Bei der DNA-Replikation wird eine identische Kopie der DNA hergestellt, um sie vor der Zellteilung weiterzugeben. Dieser Prozess ist semikonservativ: Jeder neue DNA-Strang besteht aus einem alten und einem neuen Strang. Phasen der Replikation: Initiation: Die Helikase entwindet die DNA-Doppelhelix und trennt die Stränge an der Replikationsgabel. Primase synthetisiert kurze RNA-Primer als Startpunkte für die Synthese. Topoisomerase verhindert Überdrehungen der DNA. Elongation: Die DNA-Polymerase III verlängert die neuen DNA-Stränge: Leitstrang (Leading Strand): kontinuierliche Synthese in 5' → 3'-Richtung. Folgestrang (Lagging Strand): diskontinuierliche Synthese in Form von Okazaki-Fragmenten. RNA-Primer werden durch DNA-Polymerase I entfernt, und Lücken werden aufgefüllt. Ligase verknüpft die Okazaki-Fragmente. Termination: Der Prozess endet, wenn zwei identische DNA-Moleküle entstehen. Bei eukaryotischen Zellen schützen Telomere die Enden der DNA. 3. Proteinbiosynthese Die Proteinbiosynthese ist der Prozess, bei dem die genetische Information der DNA über RNA in Proteine übersetzt wird. Sie besteht aus zwei Hauptschritten: Transkription und Translation. 3.1 Transkription Definition: Die DNA wird in eine Messenger-RNA (mRNA) umgeschrieben. Phasen der Transkription: Initiation: Die RNA-Polymerase bindet an den Promotor (z. B. TATA-Box) und öffnet die DNA-Doppelhelix. Elongation: Die RNA-Polymerase synthetisiert die mRNA in 5' → 3'-Richtung, wobei sie die Basen der DNA abliest (A → U, T → A, G ↔ C). Termination: Am Terminator-Stopp-Punkt wird die mRNA freigesetzt. Bei Eukaryoten entsteht zunächst eine prä-mRNA. Prozessierung der prä-mRNA (nur bei Eukaryoten): Capping: Hinzufügen einer Kappe am 5'-Ende (Schutz und Regulation). Polyadenylierung: Hinzufügen eines Poly-A-Schwanzes am 3'-Ende. Splicing: Entfernung von Introns (nicht codierende Abschnitte) und Verknüpfung der Exons (codierende Abschnitte). Ergebnis: Fertige mRNA für die Translation. 3.2 Translation Definition: Die mRNA wird an den Ribosomen in eine Aminosäurekette (Polypeptid) übersetzt. Ablauf: Initiation: Die kleine ribosomale Untereinheit bindet an das 5'-Ende der mRNA und wandert zum Startcodon AUG. Die passende tRNA bringt Methionin (Met) und bindet über das Anticodon. Die große ribosomale Untereinheit bildet den Initiationskomplex. Elongation: tRNA-Moleküle binden an die mRNA-Codons an der A-Stelle. Peptidbindungen zwischen Aminosäuren werden gebildet, die Kette wächst. Das Ribosom bewegt sich ein Codon weiter (tRNA von A- zu P- und dann zur E-Stelle). Termination: Erreicht das Ribosom ein Stopcodon (UAA, UAG, UGA), bindet ein Freisetzungsfaktor. Die Polypeptidkette wird freigesetzt, das Ribosom zerfällt. Codesonne: Jedes Codon (Basentriplett) codiert für eine Aminosäure. Startcodon: AUG (Methionin), Stopcodons: UAA, UAG, UGA. 4. Ergebnis Die Proteinbiosynthese führt zur Bildung von Proteinen, die als Enzyme, Strukturproteine oder Transportproteine eine Vielzahl biologischer 2. Gesundheit und Krankheit Definitionen Gesundheit: Laut WHO ist Gesundheit „ein Zustand des vollständigen körperlichen, geistigen und sozialen Wohlbefindens und nicht nur das Fehlen von Krankheit oder Gebrechen“. Krankheit: Eine Störung der normalen physischen oder psychischen Funktionen, die die Leistungsfähigkeit und das Wohlbefinden negativ beeinflusst. Unterschied zwischen Gesundheit und Krankheit Es gibt fließende Übergänge, z. B. bei chronischen Krankheiten, Behinderungen oder psychischen Belastungen. Beispiele für Gesundheitszustände oder Krankheiten: Krankheiten: Allergien, Depressionen, Nikotinsucht, Karies, Übergewicht. Umstritten: Stress oder leichte Akne gelten oft nicht direkt als Krankheiten. Behinderung Eine dauerhafte Funktionsstörung, die die Teilhabe am gesellschaftlichen Leben erheblich einschränkt. Unterscheidung zwischen angeborenen und erworbenen Behinderungen. Gesundheitssystem in Österreich Universeller Zugang: Alle Bürger, von Arbeitnehmern bis zu Studierenden, sind durch Pflichtversicherungen abgedeckt. Gesundheitsleistungen sind oft kostengünstig oder gratis. Solidaritätsprinzip: Beiträge sind einkommensabhängig, aber die Leistungen für alle gleich. Leistungen der Krankenversicherung: Prävention (z. B. Vorsorgeuntersuchungen). Behandlung (z. B. Medikamente, Arztbesuche). Mutterschaft (z. B. Wochengeld). Private Krankenversicherung: Zusatzleistungen wie Wahlärzte, Einbettzimmer, Zahnarztkosten. Gesundheitsziele in Österreich Ziele: Verbesserung der Lebensqualität und Erhöhung der gesunden Lebensjahre. Eindämmung steigender Gesundheitskosten. Maßnahmen: Förderung gesunder Lebensweisen, z. B. durch Bewegungsprogramme oder Präventionskampagnen. 3. Antibiotikaresistenzen Entstehung von Resistenzen Natürliche Resistenz: Manche Bakterien sind von Natur aus unempfindlich gegenüber bestimmten Antibiotika. Erworbene Resistenz: Entsteht durch Mutationen oder den Erwerb resistenter Gene über horizontalen Gentransfer (z. B. über Plasmide). Mechanismen der Resistenz Veränderte Zielstrukturen: Antibiotika können nicht mehr an ihren Zielort binden. Inaktivierung von Antibiotika: Enzyme wie Beta-Laktamasen zerstören Antibiotika. Efflux-Pumpen: Bakterien pumpen Antibiotika aktiv aus der Zelle. Verstärkte Schutzmechanismen: Veränderungen der Zellmembran verhindern das Eindringen von Antibiotika. Herausforderungen durch Resistenzen Multiresistente Erreger wie MRSA oder ESBL stellen ein wachsendes Problem dar. Übermäßiger Einsatz von Antibiotika in der Medizin und Landwirtschaft beschleunigt die Entwicklung von Resistenzen. 4. Infektionskrankheiten Allgemeines Infektionskrankheiten sind durch Krankheitserreger ausgelöste, ansteckende Krankheiten. Sie unterscheiden sich von normalen Infektionen durch die Manifestation von Symptomen. Krankheitserreger Bakterien: Beispiele: Cholera, Salmonellen, Tuberkulose. Viren: Beispiele: Grippe, Hepatitis, HIV, COVID-19. Pilze: Beispiele: Hefepilze, Schimmelpilze. Parasiten: Beispiele: Malaria (Protozoen), Würmer. Prionen: Beispiele: Creutzfeldt-Jakob-Krankheit, BSE. Phasen einer Infektionskrankheit Infektion: Eindringen des Erregers in den Körper. Inkubationszeit: Zeit zwischen Infektion und Auftreten erster Symptome. Krankheit: Symptome entwickeln sich. Therapie oder Gesundung: Der Körper heilt, oft unterstützt durch Medikamente. Infektionswege Tröpfcheninfektion: Übertragung durch Husten, Niesen, Sprechen. Schmierinfektion: Übertragung über kontaminierte Gegenstände oder direkten Kontakt. Lebensmittelinfektion: Über verunreinigte Nahrung (z. B. rohe Eier, verschmutztes Wasser). Direkte Blutinfektion: Über Spritzen oder Parasiten (z. B. Zecken). Schutzmaßnahmen Persönliche Hygiene: Händewaschen, Schutzmasken. Öffentliche Hygiene: Kontrolle von Wasser- und Lebensmittelqualität. Impfungen: Prävention gegen spezifische Erreger. Stärkung des Immunsystems: Gesunde Ernährung, Bewegung.

BIOL 1140 Chapters 15-16 Review Worksheet KEY Define transcription Transcription is the process of creating RNA from DNA. Describe how only one strand of DNA is used as the template in transcription. Only one of the strands (3’-5’ strand) serves as a template; the other strand is unused. Identify the three steps of transcription and briefly what is happening in each step. Initiation - in this step, the enzyme *RNA polymerase attaches to a region of the gene called a promoter, and transcription starts Elongation – In elongation, the enzyme RNA polymerase zips along the DNA strand adding complementary nucleotides to the DN template. The newly made RNA is fed out the back of the enzyme, and the two DNA strands re-anneal (re-zip). Remember that adenine, guanine, and cytosine are used in making RNA, but uracil is used in place of thymine. Termination - in this step, RNA polymerase reaches a sequence of nucleotides on the DNA template called a terminator. RNA polymerase then detaches from the newly synthesized RNA and the DNA. *before RNA polymerase binds, a series of proteins called transcription factors first bind to the promoter. Once they bind, they “recruit” RNA polymerase to the promoter. The binding of RNA polymerase starts the transcription process Which of the following statements regarding transcription is not true? A. The three stages of transcription are initiation, elongation and termination B. The key enzyme responsible for transcription is RNA polymerase C. Transcription is the conversion of information from DNA nucleotides into RNA nucleotides D. Transcription in eukaryotes is regulated (in part) by the binding of transcription factors to the promoter E. All are true statements What is the name of the enzyme used in transcription? Where does this enzyme bind? RNA polymerase…it binds to the gene’s promoter (though it doesn’t bind directly to the DNA strand) Indicate if the following statements about codons, amino acids and the genetic code are true or false: ____True______ A codon is a three nucleotide sequence that codes for a specific amino acid ____ True ______ In the genetic code, a codon will code for only one amino acid; that is there is specificity on the genetic code. ____False______ Some codons consist of only two nucleotides. 🡪 all are three nucleotides _____False_____ Some amino acids are not specified by any codons. 🡪 all amino acids have their own set of codons ____ True ______ Some codons (“stop codons”) do not code for any amino acid. ____ True ______ More than one codon can code for the same amino acid; that is, there is redundancy in the genetic code. Define translation. Translation is the process of creating proteins from RNA. Match the key players in translation with their function Answers B_____ tRNA A) The kind of RNA that makes up a ribosome. D______ mRNA B) Acts as the ‘interpreter’ in translation, by bringing in amino acids. C_______ DNA C) The genetic information in a cell. A_______ rRNA D) The kind of RNA that codes for amino acids. E_______ Ribosome E) Where translation takes place. Identify the three steps of translation and briefly describe what is happening in each step. Initiation – First an mRNA molecule binds to the small ribosomal subunit. A special initiator tRNA binds to a specific codon called the start codon (AUG = methionine). The initiator tRNA which carries the amino acid methionine, binds its anticodon (UAC) to the start codon . Second, a large ribosomal subunit binds to the small one, creating a function ribosome. The initiator tRNA binds to one of two tRNA binding sites on the ribosome. Elongation - In elongation amino acids are added one-by-one to the first amino acid. Each addition occurs in a three-step process: 1st: the anticodon of an incoming tRNA molecule, carrying its amino acid, pairs with the mRNA codon. 2nd: the incoming amino acid attaches by peptide bond to the amino acid already present – the formation of the bond is catalyzed by the ribosome. 3rd : The tRNA already present moves over to the next site (the codon and anticodon remain hydrogen bonded and the mRNA and tRNA move over as a unit), allowing another tRNA to move in. The second amino acid is then added to the growing polypeptide chain. The process is repeated - the first tRNA leaves the ribosome, the second tRNA moves over, allowing room for the next to move in…the process is repeated over and over again Termination - Elongation continues until a stop codon reaches the ribosome (recall that a stop codon does not code for any amino acid). The completed polypeptide is freed from the tRNA and the ribosome splits back into two separate subunits. Which of the following statements regarding translation is not true? A. Translation is the conversion of information from nucleic acids to proteins B. Translation takes place in the nucleus C. During translation, amino acids are linked to one another by peptide bonds D. Polypeptides made during translation must still be modified to become fully-functioning mature proteins E. All are true statements

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