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ACS BIOCHEMISTRY EXAM 2024 Questions and Verified Answers, 100% Guarantee Pass

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  • ACS Biochemistry
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  • ACS Biochemistry

ACS BIOCHEMISTRY EXAM 2024 Questions and Verified Answers, 100% Guarantee Pass

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  • September 5, 2024
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ACS BIOCHEMISTRY EXAM-.pdf file:///C:/Users/HP/Desktop/New%20folder/ACS%20BIOCHEMIS




ACS BIOCHEMISTRY EXAM


1. Henderson-Hasselbach Equation

Answer pH = pKa + log ([A-] / [HA])

2. FMOC Chemical Synthesis

Answer Used in synthesis of a growing amino acid chain toa polystyrene bead. FMOC is used as

a protecting group on the N-terminus.

3. Salting Out (Purification)

Answer Changes soluble protein to solid precipitate. Proteinprecipitates when the charges on

the protein match the charges in the solution.

4. Size-Exclusion Chromatography

Answer Separates sample based on size with smallermolecules eluting later.

5. Ion-Exchange Chromatography

Answer Separates sample based on charge. CM at-tracts +, DEAE attracts -. May have

repulsion effect on like charges. Salt or acid used to remove stuck proteins.

6. Hydrophobic/Reverse Phase Chromatography

Answer Beads are coated with a car-bon chain. Hydrophobic proteins stick better. Elute with





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non-H-bonding solvent (acetonitrile).

7. Affinity Chromatography

Answer Attach a ligand that binds a protein to a bead. Elutewith harsh chemicals or similar

ligand.

8. SDS-PAGE

Answer Uses SDS. Gel is made from cross-linked polyacrylamide. Separatesbased off of mass with

smaller molecules moving faster.Visualized with Coomassieblue.

9. SDS

Answer Sodium dodecyl sulfate. Unfolds proteins and gives them uniform negativecharge.

10. Isoelectric Focusing

Answer Variation of gel electrophoresis where protein charge matters. Involves electrodes and

pH gradient. Protein stops at their pI when neutral.

11. FDNB (1-fluoro-2,3-dinitrobenzene)

Answer FDNB reacts with the N-terminus of theprotein to produce a 2,4-dinitrophenol

derivative that labels the first residue. Can repeat hydrolysis to determine sequential amino

acids.

12. DTT (dithiothreitol)

Answer Reduces disulfide bonds.





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13. Iodoacetate

Answer Adds carboxymethyl group on free -SH groups. Blocks disulfidebonding.

14. Homologs

Answer Shares 25% identity with another gene

15. Orthologs

Answer Similar genes in different organisms

16. Paralogs

Answer Similar "paired" genes in the same organism

17. Ramachandran Plot

Answer Shows favorable phi-psi angle combinations. 3 main"wells" for ±h-elices, ß-sheets,

and left-handed ±h-elices.

18. Glycine Ramachandran Plot

Answer Glycine can adopt more angles. (H's forR-group).

19. Proline Ramachandran Plot

Answer Proline adopts fewer angles. Amino group isincorporated into a ring.









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20. ±h-elices

Answer Ala is common, Gly & Pro are not very common. Side-chain inter- actions every 3

or 4 residues. Turns once every 3.6 residues. Distance betweenbackbones is 5.4Å.

21. Helix Dipole

Answer Formed from added dipole moments of all hydrogen bonds in an

±h-elix. N-terminus is ´+and C-terminus is ´-.

22. ß-sheet

Answer Either parallel or anti-parallel. Often twisted to increase strength.

23. Anti-parallel ß-sheet

Answer Alternating sheet directions (C & N-termini don't line-up).Has straight H-bonds.

24. Parallel ß-sheet

Answer Same sheet directions (C & N-termini line up). Has angledH-bonds.

25. ß-turns

Answer 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.

26. Loops

Answer Not highly structured. Not necessary highly flexible, but can occasionallymove. Very







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