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ACS BIOCHEMISTRY EXAM 2024/ACTUAL EXAM WITH 250 QUESTIONS AND CORRECT VERIFIED ANSWERS/LATEST UPDATE

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ACS BIOCHEMISTRY EXAM 2024/ACTUAL EXAM WITH 250 QUESTIONS AND CORRECT VERIFIED ANSWERS/LATEST UPDATE

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  • August 29, 2024
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  • 2024/2025
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  • acs biochemistry exam 2024actual exam with 250 qu

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ACS BIOCHEMISTRY EXAM 2024/ACTUAL EXAM WITH
250 QUESTIONS AND CORRECT VERIFIED
ANSWERS/LATEST UPDATE 2024-2025

Henderson-Hasselbach Equation - SOLUTION:->>>- pH = pKa + log ([A-] / [HA])


FMOC Chemical Synthesis - SOLUTION:->>>- Used in synthesis of a growing

amino acid chainto a polystyrene bead. FMOC is used as a protecting group on

the N-terminus.



Salting Out (Purification) - SOLUTION:->>>- Changes soluble protein to solid

precipitate. Proteinprecipitates when the charges on the protein match the charges

in the solution.




Size-Exclusion Chromatography - SOLUTION:->>>- Separates sample

based on size with smaller molecules eluting later.



Ion-Exchange Chromatography - SOLUTION:->>>- Separates sample based on

charge. CM attracts +, DEAE attracts -. May have repulsion effect on like charges.

Salt or acid used to remove stuck proteins.



Hydrophobic/Reverse Phase Chromatography - SOLUTION:->>>- Beads

are coated with a carbon chain. Hydrophobic proteins stick better. Elute with

,non-H-bonding solvent (acetonitrile).



Affinity Chromatography - SOLUTION:->>>- Attach a ligand that binds a protein

to a bead. Elute with harsh chemicals or similar ligand.




SDS-PAGE - SOLUTION:->>>- Uses SDS. Gel is made from cross-linked

polyacrylamide. Separates based off of mass with smaller molecules moving

faster. Visualized with Coomassie blue.



SDS - SOLUTION:->>>- Sodium dodecyl sulfate. Unfolds proteins and

gives them uniform negative charge.




Isoelectric Focusing - SOLUTION:->>>- Variation of gel electrophoresis

where protein charge matters. Involves electrodes and pH gradient. Protein

stops at their pI when neutral.




FDNB (1-fluoro-2,3-dinitrobenzene) - SOLUTION:->>>- FDNB reacts with the

N-terminus of the protein to produce a 2,4-dinitrophenol derivative that labels the

first residue. Can repeat hydrolysis to determine sequential amino acids.




DTT (dithiothreitol) - SOLUTION:->>>- Reduces disulfide bonds.

,Iodoacetate - SOLUTION:->>>- Adds carboxymethyl group on free -SH groups.

Blocks disulfide bonding.




Homologs - SOLUTION:->>>- Shares 25% identity with another gene



Orthologs - SOLUTION:->>>- Similar genes in different organisms



Paralogs - SOLUTION:->>>- Similar "paired" genes in the same organism



Ramachandran Plot - SOLUTION:->>>- Shows favorable phi-psi angle

combinations. 3 main "wells" for α-helices, ß-sheets, and left-handed α-

helices.




Glycine Ramachandran Plot - SOLUTION:->>>- Glycine can adopt more angles.

(H's for R- group).




Proline Ramachandran Plot - SOLUTION:->>>- Proline adopts fewer angles.

Amino group is incorporated into a ring.




α-helices - SOLUTION:->>>- Ala is common, Gly & Pro are not very common.

Side-chain interactions every 3 or 4 residues. Turns once every 3.6 residues.

, Distance betweenbackbones is 5.4Å.



Helix Dipole - SOLUTION:->>>- Formed from added dipole moments of all

hydrogen bonds in anα-helix. N-terminus is δ+ and C-terminus is δ-.




ß-sheet - SOLUTION:->>>- Either parallel or anti-parallel. Often twisted to

increase strength.



Anti-parallel ß-sheet - SOLUTION:->>>- Alternating sheet directions (C & N-

termini don't line-up). Has straight H-bonds.




Parallel ß-sheet - SOLUTION:->>>- Same sheet directions (C & N-termini line

up). Has angled H-bonds.




ß-turns - SOLUTION:->>>- Tight u-turns with specific phi-psi angles. Must have

gly at position 3. Proline may also be at ß-turn because it can have a cis-omega

angle.




Loops - SOLUTION:->>>- Not highly structured. Not necessary highly

flexible, but canoccasionally move. Very variable in sequence.

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