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
1|Page
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
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
3|Page
The benefits of buying summaries with Stuvia:
Guaranteed quality through customer reviews
Stuvia customers have reviewed more than 700,000 summaries. This how you know that you are buying the best documents.
Quick and easy check-out
You can quickly pay through credit card or Stuvia-credit for the summaries. There is no membership needed.
Focus on what matters
Your fellow students write the study notes themselves, which is why the documents are always reliable and up-to-date. This ensures you quickly get to the core!
Frequently asked questions
What do I get when I buy this document?
You get a PDF, available immediately after your purchase. The purchased document is accessible anytime, anywhere and indefinitely through your profile.
Satisfaction guarantee: how does it work?
Our satisfaction guarantee ensures that you always find a study document that suits you well. You fill out a form, and our customer service team takes care of the rest.
Who am I buying these notes from?
Stuvia is a marketplace, so you are not buying this document from us, but from seller Brightstars. Stuvia facilitates payment to the seller.
Will I be stuck with a subscription?
No, you only buy these notes for $11.49. You're not tied to anything after your purchase.
