BCH 451 Final Exam Questions And
Answers 100% Pass
The _____ describes the relation between the interatomic distances, electronic charge,
solution dielectric, and free energies. - answer✔van der Waals interaction
Protein ____ structure defines the relationship among subunits in a multisubunit lattice -
answer✔Quaternary
Protein _____ structure defines amino acid sequence - answer✔Primary
Protein _____ structure defines the packing of helices, sheets, turns, etc. - answer✔Tertiary
Protein ____ structure defines motifs formed by short range interactions between amino
acids - 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. - answer✔hydrogen bond
____ is used to determine the sequence of a protein based on sequential chemical reactivity.
- answer✔Edman degradation
A ____ induces denaturation of proteins by disturbing the hydrophobic effect. -
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. -
answer✔Ramachandran plot
A ____ has two charges which neutralize each other. - answer✔Zwitterion
____ is the primary force of potein structural stabilization. - 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. - answer✔Initial rate
An act of ____ does not change an enzyme and lowers the transition state free energy of the
associated reaction. - answer✔Catalysis
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The ____ of an enzymatic catalysis reaction is the rate achieved when it is saturated with
substrate. - answer✔Maximum velocity
The ____ or ____ equation defines the parameters that are used to characterize the kinetics of
an enzyme. - answer✔Lineweaver-Burk; double reciprocal
K(m), the substrate concentration when V0=Vmax/2, is also called ____ . -
answer✔Michaelis-Menten constant
A ____ is the enzyme-substrate combination formed during an enzyme catalysis event. -
answer✔Michaelis complex
The catalytic rate constant of an enzyme is abbreviated as ___. - answer✔k(cat)
____ inhibition of enzyme catalysis occurs when the inhibitor binds to the active site of the
enzyme - answer✔Competitive
____ inhibition of enzyme catalysis occurs when the inhibitor only binds to the enzyme-
substrate complex. - answer✔Uncompetitive
The ____ postulates that a constant input feed of substrate is supplied whose rate equals
that of prouct formation. - answer✔Steady state approximation
Two internal factors that limit the velocity of an enzymatic reaction are ____ and _____. -
answer✔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 ____. -
answer✔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? - answer✔serine, hydroxylate
____ reactivates acetylcholine esterase, functioning as a ______. - answer✔Pyridine
aldoximine methiodide; Nerve gas antidote
What kind of reaction produces the reactivated enzyme (for the acetylcholine esterase)? -
answer✔Nucleophilic substitution
The bisubstrate-enzyme ______ reaction is used by ____ (enzyme type) in the exchange of an
amino group for a carbonyl group between two progressively binding substrates. -
answer✔Ping pong; transaminases
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