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BCH 451 Final Exam Exam Study Guide.

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BCH 451

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BCH 451

©BRIGHTSTARS EXAM SOLUTIONS 11/15/2024 11:57 AM 1 | P a g e BCH 451 Final Exam Exam Study Guide. Van der waals interaction - answerThe () describes the relation between inter atomic distances, electronic charge, solution dielectric and free energy. Quaternary structure - answerProtein () def...

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©BRIGHTSTARS EXAM SOLUTIONS

11/15/2024 11:57 AM

BCH 451 Final Exam Exam Study Guide.

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
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, ©BRIGHTSTARS EXAM SOLUTIONS

11/15/2024 11:57 AM

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

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, ©BRIGHTSTARS EXAM SOLUTIONS

11/15/2024 11:57 AM

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

tyrosine, threonine - answer✔Which two amino acids are modified in the reactions
catalyzed by the enzyme in question 35?

noncovalent modifications, pH and pKa changes, salt changes - answer✔Two examples of
reversible factors that control the catalytic capability of an enzyme are:

covalent modification, proteolysis, irreversible inhibitors - answer✔Two examples of
irreversible factors that control the catalytic capability of an enzyme are:

Arrhenius - answer✔The () equation accounts for the temperature dependence of the rate
of the reaction

acid-base, covalent - answer✔List the two "chemical modes" of catalysis

proximity effect, transition-state stabilization - answer✔List the two "binding modes of
catalysis"

nucleophile - answer✔A () attacks an electropositive site in its role in a chemical
(enzymatic) reaction

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