General Sciences Booster

What are the types of chemical bonds?

• Ionic- strongest

• covalent- polar or nonpolar sharing of e-

• H bonding- must be a H bonded to FON, bonded to another H

• Vann Der Waals- weak interactions between molecules, stronger with larger molecules

What are the properties of Water?

• Very polar, good solvent

• high heat capacity

• denser as a liquid than solid

• cohesion

• adhesion

micromolecules: what are minerals and their function?

• inorganic ions that function in bone development, electrochemical gradients, and hemoglobin (K and Ca)

micromolecules: what are vitamins and what are their function?

• Fat soluble: deposited in fat

  ‣ Vitamin A: visual pigment and epithelial maintenance.

  ‣ Vitamin D: regulates calcium levels by promoting absorption from the intestine synthesized when UV light strikes the skin.

  ‣ Vitamin E: Antioxidant (neutralizes free radicals that can damage cells).

  > Vitamin K: blood clotting.

• Water soluble: excreted by the body

  • Vitamin B: coenzymes or precursors to coenzymes

  • Vitamin C: important for collagen synthesis

macromolecules: what is the process by which monomers combine to form polymers, producing an H2O molecule?

dehydration synthesis

macromolecules: what is the process by which an H2O molecule is used to break polymer linkages.

hydrolysis

Carbohydrates: function, monomer, polymer, and linkage type

• energy storage and structure

• monosaccharide

• polysaccharide

• glycosidic bonds

what are the common monosacharides?

glucose, fructose, galactose

what are the common disaccharides and their moosaccharides?

• sucrose- glucose and fructose

• lactose- glucose and galactose

• maltose- glucose and glucose

what are the common polysaccharides and their glicosidic bond type?

• A linked

  • starch- energy storage in plants

  • glucose- energy storage in animals

• B linked

  • cellulose- structure in plants

  • chitin- structure in fungi and arthropods

As far as carbohydrate hydrolysis, what bonds can humans not cleave? (cows use bacteria in their gut to cleave)

B linked glycosidic bonds

Lipids: function, monomer, polymer, linkage type

• nonpolar hydrophobic molecules for insulation, energy storage, cell structure, endocrine molecules, and membrane structure.

• hydrocarbon “monomer“

• hydrocarbon chain (note: lipids are not true polymers because they lack repeating monomer units).

• covalent C-C bonds

what are the types of lipids?

• triglycerides- 3 fatty acid chains connected by ester linkages to a glycerol

• phospholipids- 2 fatty acid chains connected by ester linkages to a glycerol

• steroids- four hydrocarbon rings forming hormones, cholesterol, vitamin D and bile

• porphyrins- 4 pyrrole rings with a central metal atom (chlorophyll and hemoglobin)

what is the difference between saturated and unsaturated fatty acid chains?

• Saturated- “with Hs“ no double bonds, no kinks, more intermolecular interactions, higher MP and BP, less fluid, stack densely forming fat plaques

• unsaturated- cis double bonds kink the chain, less interactions, loose fluidity, lower MP and BP

how does cholesterol affect membrane fluidity?

• cold temps- cells add cholesterol to the membrane to prevent cell stiffness

• warm temps- cells add cholesterol and saturated fatty acids to prevent excess fluidity

nucleic acids: function, monomer, polymer, linkage

• encode, express, and store genetic info

• nucleotide

• nucleic acid (RNA/DNA)

• linkage- phosphodiester bond

what is the structure of a nucleotide? DNA and RNA

• nitrogenous base + 5C sugar + phosphate

• DNA- H attached to 2’ C of sugar

• RNA- OH attached to sugar

what are the nitrogenous bases and structure of DNA?

double stranded helix with base pairs AT GC

what are the nitrogenous bases and structure of RNA?

singe stranded with pairs AU GC

how many bonds are between A-T base pairs?

2 H bonds

how many bonds are between G-C base pairs

3 H bonds

Proteins: Function, monomer, polymer, linkage type

• structure, transport, defense, storage, enzymes

• amino acids

• peptide

• peptide bonds

what is primary protein structure?

linear sequence of amino acids

gives all protein folding info

what is protein secondary structure?

A helix and B sheet folding of the primary amino acid chain. Localized and made by H bonds

what is protein tertiary structure?

3D shape of the peptide due to interations between R groups

• non covalent interactions like nonpolar on the inside and polar on the outside

• covalent interactions like disulfide bonds

what is protein quaternary structure?

3D shape of a protein consisting of multiple peptides

what is the function of the Nucleus?

Contains the cell’s DNA, and coordinates cell activities such as protein synthesis & reproduction

• in prokareotes, nucleiod contains genetic material

what is the function of the nucleolus?

site of ribosome (RNA) synthesis

what is the function of the cytoplasm?

The fluid-filled area in which the cell's metabolic activities occur; also includes the organelles

what is the function of the mitochondria?

double layered, makes ATP, site of fatty acid catabolism. Has own circular DNA and ribosomes

what is the function of ribosomes?

made of RNA, make proteins

what is the function of the rough ER?

Has ribosomes attached to the structure. Functions to synthesize and store proteins.

what is the function of the smooth ER?

synthesize lipids and steroid hormones for export

what is the function of the golgi?

Modifies and packages proteins (i.e., glycosylate polypeptides)

what are the functions of lysosomes?

Made by Golgi. Functions in apoptosis, and break down of nutrients, bacteria, and debris

what is the function of peroxisomes?

Common in the liver & kidney that

function to breakdown substances/toxins

what is the function of the cytoskeleton?

Maintain cell shape & movement

what are the components of the cytoskeleton?

• microtubules: tubulin, cell activity mobility

  • centrioles develop spindle fibers

  • cilia are hairlike extensions for movement

  • flagella are threadlike extensions for movement.

• intermediate fibers: maintain cell shape

• microfilaments- actin, cell motility

what are the characteristics of SN2 reactions?

• bimolecular

• require a strong nucleophile and aprotic solvent

• less steric hindrance faster, NR 3deg C

• pentavalent transition state

• stereocenter inversion

• rate law= k[substrate][nucleophile]

what are some strong nucleophiles/bases (used in Sn2 and E2) rxns

N3, CN, HO, RO, H2N, R2N

• negatively charged

what are some polar aprotic solvents used in Sn2 rxns?

DMSO, Acetone, THF

what are the characteristics of an E2 rxn?

• bimolecular elimination resulting in alkene formation

• Zaitsev/ more substituted alkene is preferred, less sub is made when the base is bulky(tertbutok)

• rxn can occur on 1,2,and 3 degree substrates

• the leaving group and H atom must be antiperiplanar

• requires a strong base/nucleophile

• requires a polar protic solvent and heat

what are examples of polar protic solvents?

H20. ROH, NH3

what are the characteristics of an Sn1 RXN?

• weak nucleophile w/o neg chg (H2O, ROH)

• rearrangement possible, carbocation formation

• polar protic solvent favored as H bonds stabilize carbocation

• rate law k=[substrate]

what are the characteristics of an E1 rxn?

• weak base/nucleophile (H2O, ROH)

• carbocation intermediate

• polar protic solvent and heat

• zaitsev product is favored

• rate law= k[substrate]

What are EAS ortho/para directors?

• activating groups

• electron donating groups

  • NH2, NR2

  • OH, OR

  • NHCOR

  • CH3, R group

• weak electron withdrawing groups

  • Halogens

what are EAS meta directors?

• Deactivating groups

• moderate and strong electron withdrawing groups

  • carboxyl groups with R,OH,or OR group

  • SOH3, CN, NO2, NH2R3, CF3

what is the bromine test OCHM?

• BR2 or CCL4

• tests for alkenes and alkynes

• positive= brown dissapears

what is the Baeyer test OCHM?

• KMNO4 dilute

• tests for alkanes and alkenes

• Positive= purple to brown

what is the silver nitrate in alcohol test OCHM?

• AgNO3 in alcohol

• test for alkyl halides

• positive= precipitate

what is the iodoform test OCHM?

• I2/NaOH

• tests for methyl ketones

• positive= yellow precipitate

what is Tollen’s test OCHM?

• Ag2O/NH3

• tests for aldehydes

• positive= silver mirror

what is the Lucas test OCHM?

• ZnCl/HCl

• tests for all degrees of alcohols (benzylic as well) except primary

• cloudy appearance is positive

what is the jones test OCHM?

• CrO3/H2SO4

• tests for primary and secondary alcohols

• positive= blueish green

how do you determine the most acidic hydrogen on a molecule?

• sp hybridized is the most acidic

• sp>sp2>sp3

what is the difference between a lewis and bronstead acid?

• lewis is an electron pair acceptor

• bronstead is a proton donor

what is the function of the extracellular matrix?

provide mechanical support, most abundant in collagen

what organelles are found in plant cells not animal cells?

• cell walls

• plastids- organelles with various metabolic functions like chloroplasts for photosynthesis

what are the traits of prokaryotes?

• no nucleus

• single circular DNA

• ribosomes 50+30 = 70s

• cell walls of peptidoglycan (archea polysaccharides)

  • some may have sticky capsules

• flagella constructed as flagelin not microtubules

what is the difference between gram positive and gram negative bacteria?

• gram positive have a thick peptidoglycan wall, negative have thin peptidoglycan and an outer layer

what is the phospholipid membrane permeability?

• small uncharged molecules can pass through

• large, polar, or charged require a transporter

what are membrane channel proteins?

• hydrophillic, polar, and charge molecules

• ion channels- voltage, ligand, or mechanically gated

• porins- less specific, pass ions and polar molecules

what is passive membrane transport?

• down conc gradient, no ATP

• osmosis, facilitated diffusion, dialysis, plasmolysis, countercurrent exchange

what is active membrane transport?

• moves solute against conc gradient. uses ATP

• small ions, amino acids, monosaccharides

what are the types of endocytosis?

• phagocytosis- cell intakes a solid

• pinocytosis- cell intakes a liquid/dissolved solute

• receptor mediated pinocytosis

what is a hypertonic solution?

higher solute concentration, RBC lyse shrivel

what is a hypotonic solution?

lower solute concentration, RBC burst

what is an isotonic solution?

same solute concentration

what is an anchoring cell junction?

• desmosomes, link two cells together

what is a tight junction?

• surrounds entire cell, apical and basal surface, prevents passage of material between cells

what is a Gap junciton?

• narrow tunnels between animal cells to transfer small ions and molecules

what is an anabolic vs catabolic chemical reaction?

• anabolic- forming of a larger molecule

• catabolic- larger molecules broken into smaller ones

what is the delta G for an exergonic vs endergonic reaction?

• exergonic= -Delta G

• endergonic= +Delta G

how can non spontaneous reactions be made spontaneous through pairing to another rxn?

• ATP synthesis is very exergonic, it can be paired with another RXN

what is the difference between kinetic and potential energy?

• kinetic- energy in motion

• potential- stored energy

what is the structure of an enzyme?

• most made of proteins, some of RNA

• active site- where the substrate binds

• allosteric site- secondary site where an inhibiting or activating effector binds

what is the structure of a eukaryotic ribosome?

• 60S + 40S = 80S

what is the mechanism of an enzyme?

• substrate enters active site

• induced fit to better catalyze the rxn

• ^Enzyme Substrate complex

• activation energy of rxn is lowered

• products are released and cycle repeats

how do enzymes affect reactions?

• lower AE

• increase rate of rxn, fwd and reverse

• function depends on pH and temp

what is enzyme competitive regulation?

• enzyme binds to active site of enzyme

• can be overcome by increasing substrate concentration, theyll reach the active site more often

• Km inc, Vmax statys the same

what is enzyme noncompetitive regulation?

• substance binds to a secondary site,

• substrate can still bind but an inhibitor prevents rxn

• Km stays the same, Vmax decreases

what is ATP, how is it formed and how is it broken?

ATP stores energy generated from exergonic reactions of the ETC to fuel endergonic RXNs

energy source, formed through phosphorylation, breaking bonds via hydrolysis releases energy

in Michaelis Menten kinetics, what is Vmax?

max velocity of the rxn at peak substrate saturation

in Michaelis Menten kinetics, what is Km?

• the sustrate concentration at half Vmax

• inverse representation of binding affinity

• small Km= less substrate needed to reach Vmax, higher binding affinity

what is cellular respiration?

• oxidation of glucose via electron carriers to deposit their electrons in the ETC

• fuels chemiosmosis and production of ATP (exergonic)

what is glycolysis?

• ATP generated via direct transfer of a phosphate from another molecule

what are the important enzymes of Glycolyis/irreversable steps?

• hexokinase- the first committed step of glycolysis

  • glucose to gluc 6 phosphate using 1 ATP

• Phosphofructokinase- adds a second phosphate group, commits molecule to glycolysis

what is the net product of glycolysis?

• 2 ATP

• 2 pyruvate

what is anaerobic respiration?

• regeneration of oxidized NAD+ from NADH so that glycolysis can run

• glycolysis can run anaerobically

what are the types of anaerobic respiration/fermentation?

• Alcohol fermentation- pyruvate converted to acetylaldehyde and CO2, then ethanol.

  • plants fungi and yeast

• Lactic acid fermentation- pyruvate turns to lactate. lactate can be turned back to glucose in the liver

  • human muscle and microorganisms

what is aerobic respiration?

• oxygen required as final electron acceptor

  • glucose + 6O2 → 6CO2 + 6H2O + ATP

• steps include: glycolysis, pyruvate decarboxylation, citric acid cycle, and ETC

what is pyruvate decarboxylation?

• step 2 in aerobic respiration

• pyruvate moved from cytoplasm to mitochondrial matrix. pyruvate dehydrogenase complex (PDC) turns pyruvate to acetyl- CoA

what is the citric acid cycle?

• step 3 of aerobic respiration

• acetyl CoA enters and is used to regenerate oxaloacetate

• each cycle= CO2 + ATP + FADH2 and NADH

what is the electron transport chain?

• oxidative phosphorylation- e- passed from e- carriers (FADH2 and NADH) to other carrier proteins in the inner mitochondrial membrane generating H+ gradient

• ATP synthase is fueled by the proton motive force and uses chemiosmosis

• oxygen combines with H+ to form H2O

what are alternative energy sources when glucose is low?

• body uses other carbs, fats then protiens

• body creates glucose from non carb precursors via gluconeogenesis in the liver

• skeletal muscles store lots of glycogen

what is photosynthesis?

light energy from the sun is used to synthesize glucose. takes place in chloroplast

• chlorophyll A, B, and carotenoids absorb energy from sunlight

• photons excite electrons

• excited electrons are unstable and re-emit energy

• energy is absorbed by Chlorophyl A (PSI and PSII)

  • contains porphyn ring with Mg2+ inside

what is the anatomy of a chloroplast?

• outer membrane

• granum- stacks of thylakoids

• thylakoid membrane- location of ETC which absorbs light

• thylakoid lumen- location of photolysis and accumulation of H+

• intermembrane space

• inner membrane space

• stroma- location of calvin cycle

• stroma lamellae- cyclic phosphorylation

karyokinesis

• nuclear division

cytokinesis

• cytoplasmic division

diploid cell

• two copies of every chromosome

• homologous pairs