©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
1|Page
, ©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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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
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
1|Page
, ©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
2|Page
, ©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
