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BCH 451 Final Exam UPDATED ACTUAL Questions and CORRECT Answers

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BCH 451 Final Exam UPDATED ACTUAL Questions and CORRECT Answers van der Waals interaction interatomic distances electron charge solution dielectric free energies - CORRECT ANSWER- the ___ describes the relation between ___, ___, ___ and ___ quaternary structure

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  • November 12, 2024
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  • 2024/2025
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  • BCH 451
  • BCH 451
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BCH 451 Final Exam UPDATED ACTUAL
Questions and CORRECT Answers
van der Waals interaction
interatomic distances
electron charge
solution dielectric

free energies - CORRECT ANSWER- ✔✔the ___ describes the relation between ___, ___,
___ and ___


quaternary structure
subunits

lattice - CORRECT ANSWER- ✔✔protein ___ defines the relation among ___ in a
multisubunit ___


primary structure
amino

sequence - CORRECT ANSWER- ✔✔protein ___ defines the ___ acid ___


tertiary structure
packing

helices, sheets, turns - CORRECT ANSWER- ✔✔protein ___ defines the ___of ___, ___,
___, etc.


secondary structure
motifs
short-range

amino acids - CORRECT ANSWER- ✔✔protein ___ defines the ___formed by ___
interactions between ___


hydrogen bond

,polar O

protein stabilization - CORRECT 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 - CORRECT ANSWER- ✔✔___ is used to determine the sequence of a
___ based on sequential ___


chaotropic agent
denaturation

hydrophobic effect - CORRECT ANSWER- ✔✔a ___ induces ___ of proteins by disturbing
the ___


Ramachandran plot
conformational
residues
protein
peptide

polypeptide - CORRECT 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 - CORRECT ANSWER- ✔✔a ___ has ___ charges which ___ each other


hydrophobic effect
force

structural - CORRECT ANSWER- ✔✔the ___ is the primary "___" of protein
___stabilization


initial rate

, kinetics
substrate

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


catalysis
enzyme
lowers

transition state - CORRECT ANSWER- ✔✔an act of ___ does not change an ___ and___the
___ free energy of the associated reaction


maximum velocity
saturated

substrate - CORRECT ANSWER- ✔✔the ___ of an enzymatic catalysis reaction is the rate
achieved when it is ___ with ___


Lineweaver-Burk
double reciprocal

kinectics - CORRECT ANSWER- ✔✔the ___ (___) equation defines parameters that are
used to characterize the ___of an enzyme


Km
Vmax/2

Michaelis-Menten constant - CORRECT ANSWER- ✔✔___ is the concentration when V0 =
___, or ___


Michaelis complex
enzyme-substrate

catalysis - CORRECT ANSWER- ✔✔a ___ is the ___ combination formed during an enzyme
___ event


catalytic

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