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WGU BioChem OA Review with complete solution

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  • WGU BioChem OA
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  • WGU BioChem OA

WGU BioChem OA Review with complete solution

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  • October 3, 2024
  • 32
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers
  • WGU BioChem OA
  • WGU BioChem OA
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WGU BioChem OA Review with complete
solution


types of enzyme regulation - --ANSWER---
Phosphorylation
Dephosphyorylation
Feedback inhibition
Competitive inhibitor
Non competitive inhibitor


chaperones - --ANSWER---protein helpers that help
folding of complicated protein structure they bind to
newly made polypeptides and enable proper folding


Protein structures are stablized by: - --ANSWER---the
hydrophobic effect with van der waals interactions


Disulfide bonds can be found in: - --ANSWER---proteins
secreted from a cell: insulin
structural purpose proteins: keratin skin hair nails

,Denaturation - --ANSWER---the los of secondary,
teritary, and quatirary structure-primary structure remains
intact.
They do lose their ability to fx properly though


Why does denaturation happen? - --ANSWER---Heat
exposes hydrophobic bonds to water outside of a protein
cauisng the amino acid to clump together and aggregate


Hydrogen and Ionic bonds can be broken how? - --
ANSWER---by changes in salt and PH concentration
-protein doesn't aggregate but it does cause protein to not
be fxn.


How can disulfide bonds be broken? - --ANSWER---by
reducing agents (i.e.chemicals)


Heat breaks which bonds? - --ANSWER---Hydrophobic
interactions (effect)

,Changes in PH changes which bonds? - --ANSWER---
Ionic and hydrogen bonds


High concentrations of NA+ affects which bonds? - --
ANSWER---Ionic and H+ bonds


Primary structure is held together by which bonds? - --
ANSWER---peptide bonds


Secondary structure is held together by which bonds? - --
ANSWER---Hydrogen bonds


Teritary structure is held together by which interactions? -
--ANSWER---R-side chain interactions


What enviornmental factors affect enzyme activity? - --
ANSWER---Temp
PH
substrate concentrations
Coenzymes

, competitive inhibition - --ANSWER---a molecule that
resembles the normal substrate and competes for active
sight of the enzymes


non-competitive inhibitor - --ANSWER---Does not
interact w/substrate nor active sight of the enzyme
-Attaches to different area of the enzyme and changes the
shape of the enzyme.


Induced fit - --ANSWER---enzymes adjusting their active
site conformation slightly as the substrate bind to improve
the fit-it adjusts to form itself around the substrate more
tightly


What affects how active an enzyme is? - --ANSWER---
the closer an environment is to the optimal environment
for an enzyme, the more active it is


Cofactor/Co-enzyme - --ANSWER---an additional binder
that helps an enzyme function before it can operate4 on
the substrate

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