ACS BIOCHEMISTRY FINAL STUDY GUIDE 2026 COMPLETE QUESTIONS AND ANSWERS.

ACS BIOCHEMISTRY FINAL STUDY
GUIDE 2026 COMPLETE QUESTIONS AND
ANSWERS.




■ Edman degredation (3). Ans: used in the sequencing of polypeptides;
labels and removes ONLY the amino-residue from a polypeptide. carried
out in a machine called a sequenator


■ φ in peptide bonding (chapter 4). Ans: angle around the α-carbon -
amide nitrogen bond


■ ψ in peptide bonding (chapter 4). Ans: angle around the α-carbon -
carbonyl carbon bond


■ Ramachandran Plot (4). Ans: shows favoreable φ-ψ angle
combinations. 3 main "wells" for α-helices, β-sheets, and left handed α-
helices


■ Levinthal's Paradox (4). Ans: protein folding cannot be a completely
random, trial and error process

, ■ chaperonins (4). Ans: elaborite protein complexes required for the
folding of a number of cellular proteins that do not fold spontaneously


■ Henderson-Hasselbach Equation (2). Ans: pH = pKa + log([A-]/[HA])


■ which amino acids are not found in α-helices? (4). Ans: glycine and
proline. glycine is too flexible, proline is too rigid to rotate.


■ which amino acids are commonly found in β turns? (4). Ans: glycine,
because it is small and flexible, and proline because it forms cis
conformation in tight turns.


■ β-mercaptoethanol (4). Ans: breaks disulfide bonds


■ circular dichroism (4). Ans: technique that measures the amount of
helical structures in macromolecule (protein is denatured)


■ Acid Dissasociation constant Ka (2). Ans: quantitative measure of the
strength of an acid in solution


■ Native Fold. Ans:


■ Size-exclusion chromatography (3). Ans: Separates proteins according
to size. Large proteins emerge from the column before small ones