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BCH 451 Final Exam UPDATED Questions and CORRECT Answers
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BCH 451 Final Exam UPDATED Questions and CORRECT Answers The _____ describes the relation between the interatomic distances, electronic charge, solution dielectric, and free energies. - CORRECT ANSWER- van der Waals interaction Protein ____ structure defines the relationship among subunits in...

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  • November 12, 2024
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  • 2024/2025
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BCH 451 Final Exam UPDATED Questions
and CORRECT Answers
The _____ describes the relation between the interatomic distances, electronic charge,
solution dielectric, and free energies. - CORRECT ANSWER- ✔✔van der Waals interaction


Protein ____ structure defines the relationship among subunits in a multisubunit lattice -
CORRECT ANSWER- ✔✔Quaternary



Protein _____ structure defines amino acid sequence - CORRECT ANSWER- ✔✔Primary


Protein _____ structure defines the packing of helices, sheets, turns, etc. - CORRECT
ANSWER- ✔✔Tertiary


Protein ____ structure defines motifs formed by short range interactions between amino acids
- CORRECT ANSWER- ✔✔Secondary


A ____ involves polar O, N or both and the atom for which it is named, and constitutes one of
the important protein stabilization elements. - CORRECT ANSWER- ✔✔hydrogen bond


____ is used to determine the sequence of a protein based on sequential chemical reactivity. -
CORRECT ANSWER- ✔✔Edman degradation


A ____ induces denaturation of proteins by disturbing the hydrophobic effect. - CORRECT
ANSWER- ✔✔chaotropic agent


A _____ is a graph of the conformational torsion angles phi and upsilon for the residues in a
protein or peptide; a map of the structure of the polypeptide bakbone. - CORRECT
ANSWER- ✔✔Ramachandran plot



A ____ has two charges which neutralize each other. - CORRECT ANSWER- ✔✔Zwitterion

, ____ is the primary force of potein structural stabilization. - CORRECT ANSWER-
✔✔Hydrophobic effect


The ____ is the characteristic speed of an enzyme's kinetics extrapolated to a time when a
defined amount of substrate is added to the enzyme solution. - CORRECT ANSWER-
✔✔Initial rate


An act of ____ does not change an enzyme and lowers the transition state free energy of the
associated reaction. - CORRECT ANSWER- ✔✔Catalysis


The ____ of an enzymatic catalysis reaction is the rate achieved when it is saturated with
substrate. - CORRECT ANSWER- ✔✔Maximum velocity


The ____ or ____ equation defines the parameters that are used to characterize the kinetics of
an enzyme. - CORRECT ANSWER- ✔✔Lineweaver-Burk; double reciprocal


K(m), the substrate concentration when V0=Vmax/2, is also called ____ . - CORRECT
ANSWER- ✔✔Michaelis-Menten constant


A ____ is the enzyme-substrate combination formed during an enzyme catalysis event. -
CORRECT ANSWER- ✔✔Michaelis complex


The catalytic rate constant of an enzyme is abbreviated as ___. - CORRECT ANSWER-
✔✔k(cat)


____ inhibition of enzyme catalysis occurs when the inhibitor binds to the active site of the
enzyme - CORRECT ANSWER- ✔✔Competitive


____ inhibition of enzyme catalysis occurs when the inhibitor only binds to the enzyme-
substrate complex. - CORRECT ANSWER- ✔✔Uncompetitive


The ____ postulates that a constant input feed of substrate is supplied whose rate equals that
of prouct formation. - CORRECT ANSWER- ✔✔Steady state approximation

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