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
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
