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mcat biochem
| Question | Answer |
|---|---|
| sphingosphine | long chain amino alcohol |
| sphingolipid | sphingosine + 1 FA; ester linked; provides structure in cell membrane |
| phospholipid | glycerol + 2 FAs + charged head group; ester linked |
| TAG | glycerol + 3 FAs; ester linked |
| phosphodiester bond | covalent bond in DNA/RNA backbone; between phosphate of one nucleotide and hydroxyl of another |
| pyrmidine | cytosine and thymine/uracil, single ring |
| purine | adenine and guanine; double ring |
| ubiquitination | proteins tagged with ubiquitin, then degraded by a proteasome |
| western blot | uses antibodies to recognize proteins of interest; antibodies bind to amino acids that are close together in the folded protein |
| southern blot | detects + quanitifies specific DNA sequences |
| northern blot | detects specific RNA sequences |
| PCR | exponentially amplifies a DNA sequence to make millions of copies; needs template DNA, taq polymerase, DNA primers, and dNTPs |
| gel electrophoresis | separates molecules based on size+charge; neg. end and pos. end; smaller molecules move faster |
| SDS-PAGE | a type of gel electrophoresis; SDS denatures + gives molecules neg. charge; results determined by molecule's mass |
| native-PAGE | a type of gel electrophoresis; doesn't denature; results determined by charge |
| serine, tyrosine | most common phosphorylated AAs b/c their hydroxyl group |
| cell membrane fluidity | ↑ temp = ↑ fluidity ↓ temp = ↓ fluidity |
| unsaturated fatty acids | has cis double bond kinks which prevent tight packing to increase membrane fluidity; trans double bond increases fluidity a little bit; more prone to oxidative stress b/c double bond very reactive |
| saturated fatty acids | single bonds; reduce fluidity in membrane; have higher melting points b/c they can pack closely together and experience more Van der waals forces |
| aldose | when anomeric carbon is on carbon 1; one of substituents on anomeric carbon is H |
| ketose | when anomeric carbon is on carbon 2; no H substituents on anomeric carbon |
| reversible reactions | have ΔG° = 0 |
| urea cycle | breakdown of amino groups in proteins |
| ping pong mechanism | one substrate binds the enzyme and changes its shape; 2nd substrate binds and reverts enzyme back to orignial shape; ordered rxn |
| salt bridge | noncovalent interaction between opp. charged molecules (pos. N terminus and neg. C terminus) |
| tertiary stucture | stabilized by AA noncovalent (electrostatic) interactions between distant side chains (disulfide bonds) |
| Kd | how likely to dissociate; lower value = high affinity; higher value = low affinty |
| Beta-D-glucose | C5 OH group on the right; C1 OH group on the left |
| alpha-D-glucose | C5 OH group on the right; C1 OH group on the right |
| beta-L-glucose | C5 OH group on the left; C1 OH group on the right |
| alpha-L-glucose | C5 OH group on the left; C1 OH group on the left |
| RNA hairpins | the ones w/ more base pairs and C-G bonds are the most stable |
| phosphorylation | covalent modification |
| anion exchange chromatography | pos. charged beads, so that anions stick to column |
| ligase | puts 2 molecules together |
| lipase | breaks down lipids |
| glycine | disrupts alpha helices |
| proline | common in beta turns bc it's rigid; disrupts alpha helices |
| disulfide bond | covalent bond between cysteines that maintains tertiary structure; formed in oxidizing environments |
| primary structure | stabilized by AA covalent bonds (peptide bonds) between main chains |
| ternary complex formation | can be ordered (ligands bind in specific sequence), or random |
| holoprotein | protein w/ a prosthetic group attached that is needed for full activity |
| kinetically stable bonds | break in slow reactions (have high activation energy) |
| donor hydrogen atoms | bonded to O, N, or F; no double bonds on the electroneg. atom |
| acceptor atoms | oxygen or nitrogen, w/ at least one lone pair, don't have H attacheda |
| ATP hydrolysis | exothermic b/c more energy released from new bonds formed than from old bonds' cleavage consuming energy |
| buffering range | on titration curve, when pH = pka; curve is horizontal b/c pH changes slowly |
| water soluble vitamins | B,C |
| fat soluble vitamins | A,D,E,K |
| protease | cleave C-N peptide bond via hydrolysis |
| cysteine | only natural AA that has R configuration |
| fatty acid salts | can partially dissolve in polar and nonpolar media |
| niacin | precursor to NAD |
| enzyme active site | noncovalent bonds (H bonds, ionic bonds) so that substrate can bind reversibly |
| isoelectronic atoms | have same number of e-; the element with most neg. charge has largest atomic radius |
| ionizable group | can gain/lose an H+ |
| catalytic receptor | ligand binding causes enzymatic activity (phosphorylation) of another reaction |
| ketogenic AAs | form acetyl-CoA (lysine + leucine) |
| glucogenic AAs | form pyruvate (Asp, Ala, Glu) |
| irreversible covalent modification | proteolytic cleavage of bond; cannot be reversed |
| hydrolyzable lipids | waxes, phospholipids, TAGS, sphingolipids, glycerolipids |
| nonhydrolyzable lipids | steroids, vitamins (ADEK), prostaglandins |
| alpha helix | stabilized by hydrogen bonds in backbone between carbonyl oxygen (i) and amide hydrogen (i+4) |
| phosphorylation effect on pI | decreases pI by making molecule more neg. |
| agarose gel | large pores, used for dna separation |
| polyacrylamide gel | small pores, used for protein separation |
| amide nitrogen hybridization | always sp2 b/c resonance |
| amino acid weight | 110 Dalton |
| sanger sequencing | determines order of bases in dna sequence |
| short/medium fatty chain oxidation | in matrix |
| long fatty chain oxidation | in cytosol |
| hydropathy index | measures if molecule is hydrophobic or hydrophilic pos. score = hydrophobic neg. score = hydrophilic |
| DEHCYKR | amino acid pkas: 3-12, skip 5, 7, and 9 |
| lineweaver burk plot | slope = Km/Vmax |
| specific activity | enzyme units/1 mg of protein |
| cori cycle | connects glycolysis + gluconeogenesis; anaerobic glycolysis in muscles = lactate -> lactate converted back to glucose in liver |
| dna polymerase | synthesizes from 5' to 3' end; hydroxyl group on 3' attacks the new phosphate |
| protein isoforms | proteins that have similar functions but diff. AA sequences; causes by alternative splicing |
| adenine | 1 acceptor, 1 donor |
| thymine | 1 acceptor, 1 donor |
| guanine | (giver); 2 donors, 1 acceptor |
| cytosine | (child); 2 acceptors, 1 donor |
| helical turn | 3.6 amino acids |
| precursor of PLP | vitamin B6 |
| apoenzyme | enzyme not bound to its cofactor, and is inactive |
| holoenzyme | enzyme is bound to its cofactor, and is active |
| zymogen | enzymes that must be cleaved to become active |
| parallel beta sheets | hydrogen bonds between the amide carbonyls + NH group in backbone (adjacent backbones) |
| complex 3 ETC | ubiquinol brings e- from complex 1+2 and gives them to cytochrome c to reduce it; ubiquinol now becomes reduced form = ubiquinone |
| monoterpene | 2 isoprene units |
| squalene | 6 isoprene units |
| ionizable side chains | R,K,H,Y,C,E,D |
| find pH of weak acid soln | pH = 1/2(pka - logC) |
| find pOH of weak base soln | pOH = 1/2(pkb - logC) |
| michaelis menten curve | at low substrate concentration = first order kinetics at high substrate concentration = zero order kinetics |
| hill coefficient | greater than 1 = positive cooperativity (sigmoidal) equal to 1 = no cooperativity (hyperbolic) less than 1 = negative cooperativity |
| isoelectric focusing | anode = pos. charged cathode = neg. charged |
| peptide bond formation | -𝐧𝐮𝐜𝐥𝐞𝐨𝐩𝐡𝐢𝐥𝐢𝐜 𝐚𝐜𝐲𝐥 𝐬𝐮𝐛𝐬𝐭𝐢𝐭𝐮𝐭𝐢𝐨𝐧 as the nitrogen amine attacks the carbonyl carbon -𝐜𝐨𝐧𝐝𝐞𝐧𝐬𝐚𝐭𝐢𝐨𝐧 as the hydroxyl from carb acid leaves as a water molecule |
| phopshodiester bond | covalent bond between 5' hydroxyl and 3' phosphate; hydroxyl then attacks phosphorus atom of the next nucleotide |
| glycosidase | breaks down sugar by removing a monosaccharide via hydrolysis of a glycosidic bond |
| svedburg value | sedimentation rate; denser molecules have higher S# |
Created by:
reynangu