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ACS BIOCHEMISTRY EXAM ACTUAL 2025/2026 QUESTIONS AND 100% CORRECT ANSWERS

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ACS BIOCHEMISTRY EXAM ACTUAL 2025/2026 QUESTIONS AND 100% CORRECT ANSWERS Henderson-Hasselbach Equation - Answer -pH = pKa + log ([A-] / [HA]) FMOC Chemical Synthesis - Answer -Used in synthesis of a growing amino acid chain to a polystyrene bead. FMOC is used as a protecting group on the N-terminus. Salting Out (Purification) - Answer -Changes soluble protein to solid precipitate. Protein precipitates when the charges on the protein match the charges in the solution. Size-Exclusion Chromatography - Answer -Separates sample based on size with smaller molecules eluting later.Need assistance on Online classes, Exams & Assignments? Reach out for instant help!! Full Course Assistance, Plagiarism-free Essay Writing, Research Paper, Dissertation, Discussion Posts, etc…. Confidential & Secure services. Tutors are available for all subjects! Email now at: Ion-Exchange Chromatography - Answer -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 - Answer -Beads are coated with a carbon chain. Hydrophobic proteins stick better. Elute with non-H-bonding solvent (acetonitrile). Affinity Chromatography - Answer -Attach a ligand that binds a protein to a bead. Elute with harsh chemicals or similar ligand. SDS-PAGE - Answer -Uses SDS. Gel is made from cross-linked polyacrylamide. Separates based off of mass with smaller molecules moving faster. Visualized with Coomassie

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ACS Biochemistry Exam Questions and
Correct Solutions 2024

Describe the structural changes in hemoglobin that allow for cooperative binding of O2 - Answer -
Binding of O2 in one subunit causes a conformational change in an adjacent subunit allowing O2 to bind

Which amino acids in "a" would be charged at pH 7? - Answer -Asp, Glu, Arg, His, Lys

Which amino acids are negatively charged? - Answer -Asp, Glu

which amino acids are positively charged? - Answer -Arg, His, Lys

How are beta sheets stabilized in proteins? - Answer -Hydrogen bonding between peptide backbone
groups

Does myoglobin show cooperativity in O2 binding? If not, what structural differences account for this? -
Answer -Myoglobin does not show cooperativity because it is monomeric

What is a transition state inhibitor (how does its structure compare to the enzyme stubstrate?) how does
its affinity for the enzyme compare to the enzyme's substrate? - Answer -Similar to the substrate; binds
to the active site with greater affinity than the substrate

would it be advantageous for these potential drugs to covalently bind to the enzyme? why or why not? -
Answer -Not advantageous because the urea cycle would shut down

From a practical standpoint, would it be advantageous for these potential drugs to be less chemically
stable than the substrate? - Answer -No, because of shelf life and time to reach target

In DNA, which bases hydrogen bond? - Answer -A-T; G-C

In each base pair, how many hydrogen bonds are there? - Answer -A-T=2; G-C=3

Which base-pair would require a higher temperature to destroy the hydrogen bonds? - Answer -G-C

Based on the mechanism of alkaline hydrolysis of RNA, why is DNA less susceptible to alkaline
hydrolysis? - Answer -DNA lacks the 2' hydroxyl group

What is the difference between a reducing and nonreducing sugar? - Answer -Reducing sugars have a
free anomeric carbon that in the linear form can reduce an oxidizing agent.

what is a reducing monosaccharide? - Answer -fructose or glucose

what is a reducing disaccharide? - Answer -lactose

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