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BCH 451 Final Exam Questions and answers | Newest
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BCH 451 Final Exam Questions and answers | Newest
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BCH 451 Final Exam Questions andanswers | Newest
The _____ describes the relation between the interatomic distances, electronic charge,
ll ll ll ll ll ll ll ll ll ll
solution dielectric, and free energies. - van der Waals interaction
ll ll ll ll ll ll ll ll ll ll ll ll
Protein ____ structure defines the relationship among subunits in a multisubunit lattice -
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Quaternary
ll
ll Protein _____ structure defines amino acid sequence - Primary
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ll Protein _____ structure defines the packing of helices, sheets, turns, etc. - Tertiary
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Protein ____ structure defines motifs formed by short range interactions between amino
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acids - Secondary
ll ll ll ll ll
A ____ involves polar O, N or both and the atom for which it is named, and constitutes one
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
of the important protein stabilization elements. - hydrogen bond
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____ is used to determine the sequence of a protein based on sequential chemical
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reactivity. - Edman degradation
ll ll ll ll ll ll
A ____ induces denaturation of proteins by disturbing the hydrophobic effect. - chaotropic
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agent
ll
A _____ is a graph of the conformational torsion angles phi and upsilon for the residues in
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
a protein or peptide; a map of the structure of the polypeptide bakbone. - Ramachandran
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
plot
ll
ll A ____ has two charges which neutralize each other. - Zwitterion
ll ll ll ll ll ll ll ll ll ll ll ll
ll ____ is the primary force of potein structural stabilization. - Hydrophobic effect
ll ll ll ll ll ll ll ll ll ll ll ll ll
The ____ is the characteristic speed of an enzyme's kinetics extrapolated to a time when a
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defined amount of substrate is added to the enzyme solution. - Initial rate
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An act of ____ does not change an enzyme and lowers the transition state free energy of
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the associated reaction. - Catalysis
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The ____ of an enzymatic catalysis reaction is the rate achieved when it is saturated with
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substrate. - Maximum velocity
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The ____ or ____ equation defines the parameters that are used to characterize the
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kinetics of an enzyme. - Lineweaver-Burk; double reciprocal
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, K(m), the substrate concentration when V0=Vmax/2, is also called ____ . - Michaelis-
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Menten constant ll
A ____ is the enzyme-substrate combination formed during an enzyme catalysis event. -
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
Michaelis complex
ll ll
ll The catalytic rate constant of an enzyme is abbreviated as ___. - k(cat)
ll ll ll ll ll ll ll ll ll ll ll ll ll ll
____ inhibition of enzyme catalysis occurs when the inhibitor binds to the active site of the
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
enzyme - Competitive
ll ll ll ll ll
____ inhibition of enzyme catalysis occurs when the inhibitor only binds to the enzyme-
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substrate complex. - Uncompetitive ll ll ll ll ll
The ____ postulates that a constant input feed of substrate is supplied whose rate equals
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
that of prouct formation. - Steady state approximation
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Two internal factors that limit the velocity of an enzymatic reaction are ____ and _____. -
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hydrophobic effect, hydrogen bonding, disulfide bonds, van der Waals forces, salt bridges,
ll ll ll ll ll ll ll ll ll ll ll ll
or dipole-dipole interactions
ll ll ll
Two external factors that limit the velocity of an enzymatic reaction are ____ and ____. -
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
pH, solvent polarity, temperature, chaotropes, osmolytes, salt concentrtion
ll ll ll ll ll ll ll ll
What amino acid and functional group in the esterase site of acetylcholine esterase reacts
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with the substrate? - serine, hydroxylate
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____ reactivates acetylcholine esterase, functioning as a ______. - Pyridine aldoximine
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methiodide; Nerve gas antidote
ll ll ll ll
What kind of reaction produces the reactivated enzyme (for the acetylcholine esterase)? -
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
Nucleophilic substitution
ll ll
The bisubstrate-enzyme ______ reaction is used by ____ (enzyme type) in the exchange
ll ll ll ll ll ll ll ll ll ll ll ll ll
of an amino group for a carbonyl group between two progressively binding substrates. -
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
Ping pong; transaminases
ll ll ll
A(n) _____ works by amplifying an initial signal via several linked ____ reaction stages. -
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
Enzyme cascade; protease cleavage
ll ll ll ll
A ____ is a protein that is converted from the inactive to active forms by a covalent
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
modification, typically protease cleavage. - Zymogen
ll ll ll ll ll ll ll ll
A decrease in the activity of an enzyme as a result of binding of a product from the reaction
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in question or a subsequent reactions is referred to as ____. - Feedback inhibition
ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll ll
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