BCH 451 FINAL EXAM LATEST 2024-2025 WITH ACTUAL QUESTIONS
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van der waals interaction - ANSWER-The () describes the relation between inter
atomic distances, electronic charge, solution dielectric and free energy.
Quaternary structure - ANSWER-Protein () defines the relation among subunits
in a multisubunit lattice
primary structure - ANSWER-Protein () defines the amino acid sequence
tertiary structure - ANSWER-Protein () defines the packing of helices, sheets,
turns, etc.
secondary structure - ANSWER-Protein () defines the motifs formed by short-
range interactions between amino acids
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.
beta-sheet - ANSWER-Name the following protein structure:
,Edman degradation - ANSWER-() is used to determine the sequence of a
protein based on sequential chemical reactivity
chaotropic - ANSWER-A () agent induces denaturation of proteins by disturbing
the hydrophobic effect.
alpha helix - ANSWER-Name the following protein structure:
disulfide bond - ANSWER-Name the following protein structure:
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.
zwitterion - ANSWER-A () has two charges which neutralize each other
hydrophobic effect - ANSWER-The () is the primary "force" of protein structural
stabilization
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.
catalysis - ANSWER-An act of () does not change enzyme and lowers the
transition state free energy of the associated reaction
maximum velocity - ANSWER-The () of an enzymatic catalysis reaction is the
rate achieved when it is saturated with substrate.
,Lineweaver-Burk - ANSWER-The () (or double reciprocal) equation defines
parameters that are used to characterize the kinetics of an enzyme
Km - ANSWER-() is the substrate concentration when Vo = Vmax/2, or
Michaelis-Menten constant
Michaelis complex - ANSWER-A () is the enzyme-substrate combination formed
during an enzyme catalysis event
catalytic rate constant - ANSWER-The () of an enzyme is abbreviated as kcat.
competitive inhibition - ANSWER-() of enzyme catalysis occurs when an
inhibitor binds to the active site of the enzyme
uncompetitive inhibition - ANSWER-() of enzyme catalysis occurs when the
inhibitor only binds to the enzyme substrate complex
steady state - ANSWER-The () approximation postulates that a constant input
feed of substrate is supplied whose rate equals that of product formation
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 ()
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 ()
serine, hydroxylate - ANSWER-What amino acid and functional group in the
esterase site of acetylcholine esterase reacts with the substrate?
, Pydridine aldoximine methiodide - ANSWER-() (PAM) reactivates acetylcholine
esterase, functioning as a nerve gas antidote
nucleophilic substitution - ANSWER-What kind of reaction produces the
reactivated enzyme?
bisubstrate-enzyme - ANSWER-The () ping-pong reaction is used by
transaminases in the exchange of an amino group for a carbonyl group
between two progressively binding substrates
enzyme cascade - ANSWER-An () works by amplifying an initial signal via several
linked protease cleavage reaction states (eg blood clotting
zymogen - ANSWER-A () is a protein that is converted from inactive to active
forms by a covalent modfication, typically protease cleavage
decrease - ANSWER-A () in the activity of an enzyme as a result of binding of a
product from the reaction in question or subsequent reactions is referred to as
feedback inhibition
Allosterism - ANSWER-() involves binding of a regulatory molecule at a site
other than the active site.
Kinase and Phosphatase - ANSWER-() and () reactions, involving phosphate
addition and removal respectively, regulate both glycolysis and the Krebs Cycle
Cyclin kinase - ANSWER-() regulates entry and exit from mitosis by catalyzing a
covalent modifcation
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