BCH 451 FINAL EXAM WITH ACTUAL
QUESTIONS AND CORRECTLY WELL
DEFINED ANSWERS LATEST 2024 – 2025
ALREADY GRADED A+
The kinetics of an enzyme reaction are most easily controlled when Km is
approximately equal to ____. - ANSWERS-Actual concentration of reactant
The enzyme triose phosphate isomerase converts ____ into glyceraldehyde-3-
phosphate - ANSWERS-dihydroxyacetone phosphate
When ____ negatively regulates the phosphofructokinase-1 reaction, the general
name for this phenomenon is called ____. - ANSWERS-Citrate; Feedback inhibition
When fructose-1,6-bisphosphate stimulates the pyruvate kinase reaction the
general name for this phenomenon is ____. - ANSWERS-Feed forward activation
Protein _____ structure defines the packing of helices, sheets, turns, etc. -
ANSWERS-Tertiary
,Protein ____ structure defines motifs formed by short range interactions between
amino acids - ANSWERS-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. - ANSWERS-
hydrogen bond
____ is used to determine the sequence of a protein based on sequential
chemical reactivity. - ANSWERS-Edman degradation
The _____ describes the relation between the interatomic distances, electronic
charge, solution dielectric, and free energies. - ANSWERS-van der Waals
interaction
Protein ____ structure defines the relationship among subunits in a multisubunit
lattice - ANSWERS-Quaternary
Protein _____ structure defines amino acid sequence - ANSWERS-Primary
A ____ induces denaturation of proteins by disturbing the hydrophobic effect. -
ANSWERS-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. - ANSWERS-Ramachandran plot
A ____ has two charges which neutralize each other. - ANSWERS-Zwitterion
____ is the primary force of potein structural stabilization. - ANSWERS-
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. -
ANSWERS-Initial rate
An act of ____ does not change an enzyme and lowers the transition state free
energy of the associated reaction. - ANSWERS-Catalysis
The ____ of an enzymatic catalysis reaction is the rate achieved when it is
saturated with substrate. - ANSWERS-Maximum velocity
The ____ or ____ equation defines the parameters that are used to characterize
the kinetics of an enzyme. - ANSWERS-Lineweaver-Burk; double reciprocal
K(m), the substrate concentration when V0=Vmax/2, is also called ____ . -
ANSWERS-Michaelis-Menten constant
, A ____ is the enzyme-substrate combination formed during an enzyme catalysis
event. - ANSWERS-Michaelis complex
The catalytic rate constant of an enzyme is abbreviated as ___. - ANSWERS-k(cat)
____ inhibition of enzyme catalysis occurs when the inhibitor binds to the active
site of the enzyme - ANSWERS-Competitive
____ inhibition of enzyme catalysis occurs when the inhibitor only binds to the
enzyme-substrate complex. - ANSWERS-Uncompetitive
The ____ postulates that a constant input feed of substrate is supplied whose rate
equals that of prouct formation. - ANSWERS-Steady state approximation
Two internal factors that limit the velocity of an enzymatic reaction are ____ and
_____. - ANSWERS-hydrophobic effect, hydrogen bonding, disulfide bonds, van
der Waals forces, salt bridges, or dipole-dipole interactions
Two external factors that limit the velocity of an enzymatic reaction are ____ and
____. - ANSWERS-pH, solvent polarity, temperature, chaotropes, osmolytes, salt
concentrtion
What amino acid and functional group in the esterase site of acetylcholine
esterase reacts with the substrate? - ANSWERS-serine, hydroxylate
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