Biochemistry ACS Review Exam
Questions and Answers 100%
PASS
Henderson-Hasselbach Equation—ANSWER-how to determine pH of a
buffer
Conformation of all proteins—ANSWER-L
Zwitter ion—ANSWER-No charge
pI—ANSWER-isoelectric point net charge is zero
Order peptides deprotinate—ANSWER-1. C-termis 2. Acid Side chains 3. His
4. N-termis 5. Basic side chains
Determining protein sequence—ANSWER-edmunds degradation or mass
spec m/z
Phi—ANSWER-angle around alpha carbon of amino acids
Psi—ANSWER-angle around carbonyl carbon of a protein
Ramachandran plot—ANSWER-shows distribution of phi-psi angles in a
protein (2degree structures)
Alpha helix turn length—ANSWER-3.6 residue tun
, What favors alpha helix and why—ANSWER-Ala and leu because small and
hydrophobic so supports helix shape because side chains point outward of a
helix
what are the alpha helix breakers—ANSWER-proline because backbone
bond and Gly because its small and supports other conformations
Type 1 beta turns—ANSWER-proline in position 2 to anchor and causes cis
configuration instead of trans
Type 2 beta turns—ANSWER-gly in position 3 because its small
ka—ANSWER-association rate constant of protein + ligand
kd—ANSWER-dissociation rate constant of protein + ligand
Ka—ANSWER-equilibrium constant
Ka=ka/kd
θ—ANSWER-fraction of occupied binding sties on a protein
= [L]/[L] + kd
Kd—ANSWER-equilibrium dissociation constant
around of ligand to fill 1/2 of binding site
lower Kd—ANSWER-strong ligand-protein binding
Higher Kd—ANSWER-weak binding of protein-ligand
Enzyme—ANSWER-lowers activation energy and is not consumed
holoenzyme—ANSWER-catalytically complete enzyme
© 2026 Copyright. All Rights Reserved. This document is
protected by copyright law
Questions and Answers 100%
PASS
Henderson-Hasselbach Equation—ANSWER-how to determine pH of a
buffer
Conformation of all proteins—ANSWER-L
Zwitter ion—ANSWER-No charge
pI—ANSWER-isoelectric point net charge is zero
Order peptides deprotinate—ANSWER-1. C-termis 2. Acid Side chains 3. His
4. N-termis 5. Basic side chains
Determining protein sequence—ANSWER-edmunds degradation or mass
spec m/z
Phi—ANSWER-angle around alpha carbon of amino acids
Psi—ANSWER-angle around carbonyl carbon of a protein
Ramachandran plot—ANSWER-shows distribution of phi-psi angles in a
protein (2degree structures)
Alpha helix turn length—ANSWER-3.6 residue tun
, What favors alpha helix and why—ANSWER-Ala and leu because small and
hydrophobic so supports helix shape because side chains point outward of a
helix
what are the alpha helix breakers—ANSWER-proline because backbone
bond and Gly because its small and supports other conformations
Type 1 beta turns—ANSWER-proline in position 2 to anchor and causes cis
configuration instead of trans
Type 2 beta turns—ANSWER-gly in position 3 because its small
ka—ANSWER-association rate constant of protein + ligand
kd—ANSWER-dissociation rate constant of protein + ligand
Ka—ANSWER-equilibrium constant
Ka=ka/kd
θ—ANSWER-fraction of occupied binding sties on a protein
= [L]/[L] + kd
Kd—ANSWER-equilibrium dissociation constant
around of ligand to fill 1/2 of binding site
lower Kd—ANSWER-strong ligand-protein binding
Higher Kd—ANSWER-weak binding of protein-ligand
Enzyme—ANSWER-lowers activation energy and is not consumed
holoenzyme—ANSWER-catalytically complete enzyme
© 2026 Copyright. All Rights Reserved. This document is
protected by copyright law
