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BCH 451 FINAL EXAM QUESTIONA AND CORRECT WELL EXPLAINED ANSWERS
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BCH 451 FINAL EXAM QUESTIONA AND CORRECT WELL EXPLAINED ANSWERS
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BCH 451 FINAL EXAM QUESTIONA ANDCORRECT WELL EXPLAINED ANSWERS
QUESTION; steady state - ANSWER-The () approximation postulates that a constant input feed of
substrate is supplied whose rate equals that of product formation
QUESTION; hydrophobic effect, H-bonding, disulfide bonds, van der Waals forces, ionic bonds or dipole-
dipole interactions - ANSWER-Two internal factors that limit the velocity of an enzymatic reaction are ()
and ()
QUESTION; pH, solvent polarity, temperature, salt concentration and types, presence of chaotropes,
osmolytes - ANSWER-Two external factors that limit the velocity of an enzymatic reaction are () and ()
QUESTION; serine, hydroxylate - ANSWER-What amino acid and functional group in the esterase site of
acetylcholine esterase reacts with the substrate?
QUESTION; Pydridine aldoximine methiodide - ANSWER-() (PAM) reactivates acetylcholine esterase,
functioning as a nerve gas antidote
QUESTION;Van der waals interaction - ANSWER-The () describes the relation between inter atomic
distances, electronic charge, solution dielectric and free energy.
QUESTION; Quaternary structure - ANSWER-Protein () defines the relation among subunits in a
multisubunit lattice
QUESTION; primary structure - ANSWER-Protein () defines the amino acid sequence
QUESTION; tertiary structure - ANSWER-Protein () defines the packing of helices, sheets, turns, etc.
QUESTION; secondary structure - ANSWER-Protein () defines the motifs formed by short-range
interactions between amino acids
,QUESTION; hydrogen bond - ANSWER-A () interaction involves polar O, N or both and the atom for which
it is named, and constitutes one of the important protein stabilization elements.
QUESTION; beta-sheet - ANSWER-Name the following protein structure:
QUESTION; Edman degradation - ANSWER-() is used to determine the sequence of a protein based on
sequential chemical reactivity
QUESTION; chaotropic - ANSWER-A () agent induces denaturation of proteins by disturbing the
hydrophobic effect.
QUESTION; alpha helix - ANSWER-Name the following protein structure:
QUESTION; disulfide bond - ANSWER-Name the following protein structure:
QUESTION; Ramachandran plot - ANSWER-A () is a graph of the conformational torsion angles phi and psi
for the residues in a protein or peptide, a mal of the structure of the polypeptide backbone.
QUESTION; zwitterion - ANSWER-A () has two charges which neutralize each other
QUESTION; hydrophobic effect - ANSWER-The () is the primary "force" of protein structural stabilization
QUESTION; initial rate - ANSWER-The () is the characteristic speed of an enzyme's kinetic extrapolated to
the time when a defined amount of substrate is added to the enzyme solution.
QUESTION; catalysis - ANSWER-An act of () does not change enzyme and lowers the transition state free
energy of the associated reaction
QUESTION; maximum velocity - ANSWER-The () of an enzymatic catalysis reaction is the rate achieved
when it is saturated with substrate.
, QUESTION; Lineweaver-Burk - ANSWER-The () (or double reciprocal) equation defines parameters that
are used to characterize the kinetics of an enzyme
QUESTION; Km - ANSWER-() is the substrate concentration when Vo = Vmax/2, or Michaelis-Menten
constant
QUESTION; Michaelis complex - ANSWER-A () is the enzyme-substrate combination formed during an
enzyme catalysis event
QUESTION; catalytic rate constant - ANSWER-The () of an enzyme is abbreviated as kcat.
QUESTION; competitive inhibition - ANSWER-() of enzyme catalysis occurs when an inhibitor binds to the
active site of the enzyme
QUESTION; uncompetitive inhibition - ANSWER-() of enzyme catalysis occurs when the inhibitor only
binds to the enzyme substrate complex
QUESTION; steady state - ANSWER-The () approximation postulates that a constant input feed of
substrate is supplied whose rate equals that of product formation
QUESTION; hydrophobic effect, H-bonding, disulfide bonds, van der Waals forces, ionic bonds or dipole-
dipole interactions - ANSWER-Two internal factors that limit the velocity of an enzymatic reaction are ()
and ()
QUESTION; pH, solvent polarity, temperature, salt concentration and types, presence of chaotropes,
osmolytes - ANSWER-Two external factors that limit the velocity of an enzymatic reaction are () and ()
QUESTION; serine, hydroxylate - ANSWER-What amino acid and functional group in the esterase site of
acetylcholine esterase reacts with the substrate?
QUESTION; Pydridine aldoximine methiodide - ANSWER-() (PAM) reactivates acetylcholine esterase,
functioning as a nerve gas antidote
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