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BCH 451 Final Exam Study Guide. Van der Waals interaction interatomic distances electron charge solution dielectric free energies - answerthe ___ describes the relation between ___, ___, ___ and ___ quaternary structure subunits lattice - answerprotein ___ defines the relation among ___ in ...

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  • November 18, 2024
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©BRIGHTSTARS EXAM SOLUTIONS

11/15/2024 11:57 AM


BCH 451 Final Exam Study Guide.


Van der Waals interaction
interatomic distances
electron charge
solution dielectric

free energies - answer✔the ___ describes the relation between ___, ___, ___ and ___
quaternary structure
subunits

lattice - answer✔protein ___ defines the relation among ___ in a multisubunit ___
primary structure
amino

sequence - answer✔protein ___ defines the ___ acid ___
tertiary structure
packing

helices, sheets, turns - answer✔protein ___ defines the ___of ___, ___, ___, etc.
secondary structure
motifs
short-range

amino acids - answer✔protein ___ defines the ___formed by ___ interactions between ___
hydrogen bond
polar O



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, ©BRIGHTSTARS EXAM SOLUTIONS

11/15/2024 11:57 AM

protein stabilization - answer✔a ___ interaction involves ___, N or both and the atom for
which it is named, and constitutes one of the important ___ elements
Edman degradation
protein

chemical reactivity - answer✔___ is used to determine the sequence of a ___ based on
sequential ___
chaotropic agent
denaturation

hydrophobic effect - answer✔a ___ induces ___ of proteins by disturbing the ___
Ramachandran plot
conformational
residues
protein
peptide

polypeptide - answer✔a ___ is a graph of the ___torsion angles 'phi' and 'psi' for the ___ in a
___ or ___, a map of the structure of the ___ backbone
zwitterion
two

neutralize - answer✔a ___ has ___ charges which ___ each other
hydrophobic effect
force

structural - answer✔the ___ is the primary "___" of protein ___stabilization
initial rate
kinetics
substrate

enzyme - answer✔the ___ is the characteristic speed of an enzyme's ___ extrapolated to the
time when a defined amount of ___ is added to the ___ solution

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, ©BRIGHTSTARS EXAM SOLUTIONS

11/15/2024 11:57 AM

catalysis
enzyme
lowers

transition state - answer✔an act of ___ does not change an ___ and___the ___ free energy of
the associated reaction
maximum velocity
saturated

substrate - answer✔the ___ of an enzymatic catalysis reaction is the rate achieved when it is
___ with ___
Lineweaver-Burk
double reciprocal

kinectics - answer✔the ___ (___) equation defines parameters that are used to characterize
the ___of an enzyme
Km
Vmax/2

Michaelis-Menten constant - answer✔___ is the concentration when V0 = ___, or ___
Michaelis complex
enzyme-substrate

catalysis - answer✔a ___ is the ___ combination formed during an enzyme ___ event
catalytic

kcat - answer✔the ___ rate constant of an enzyme is abbreviated as ___
competitive inhibition
inhibitor

active site - answer✔___ of enzyme catalysis occurs when an ___ binds to the ___of the
enzyme
uncompetitive inhibition
inhibitor

3|Page

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