MIP 616 Exam 1
Multiple Choice,
MIP 616 test 1,
MIP616 Exam 1
with 100%
correct answers
already graded
A+(VERIFIED &
UPDATED)
Amino acid in polypeptides are covalently bound by what type of bond?
a) Peptide
b) protein
c) ester
,d) phosphodiester - answer peptide
An alpha helix is what kind of protein structure?
a) secondary
b) primary
c) tertiary
d) quaternary - answer secondary
If you disrupt all hydrogen bonds in a protein, what level will preserved?
a) secondary
b) primary
c) tertiary
d) quaternary - answer primary
Monomeric proteins do not contain a...
a) secondary
b) primary
c) tertiary
d) quaternary - answer quaternary
Which is not part of a zinc finger motif?
a) zinc ion
b) proline residue
c) cysteine residue
d) histidine residue - answer proline residue
a small molecule that binds directly to the active site of an enzyme and
disrupts its catalytic reaction is called:
a) an allosteric inhibitor
b) a competitive inhibitor
,c) a noncompetitive inhibitor
d) RNAi - answer a competitive inhibitor
Which statement about enzymes is TRUE?
a) The catalytic site is responsible for substrate specificity.
b) Reactions catalyzed by enzymes give the products more free energy
than reactions that occur spontaneously.
c) The rate of an enzymatic reaction is always proportional to the
concentration of the substrate
d) Enzymes increase reaction rates by lowering the activation energy
needed to reach the transition state? - answer Enzymes increase reaction
rates by lowering the activation energy needed to reach the transition
state?
Which modification marks a protein for degradation in proteasomes?
a) Phosphorylation
b) Ubiquitinoylation
c) acetylation
d) glycosylation - answer ubiquitinoylation
Kinases activates or inactivate many proteins by doing what to them?
a) methylate
b) phosphorylate
c) acetylate
d) digest - answer phosphorylate
The conversation if inactive chymoptrypsinogen to active chymotryosin is
an example of?
a) proteolytic activation
b) positive cooperativity
c) allostery
d) Ligand induced activation - answer proteolytic activation
, Which amino acid can be phosphorylated?
a) lysine
b) serine
c) glycine
d) proline - answer serine
G proteins act as...
a) a catch
b) a branch
c) a switch
d) a notch - answer a switch
what do g proteins do to their bound nucleotide triphosphate?
a) nebulize it
b) hydrolyze it
c) customize it
d) homogenize it - answer hydrolyze it
What kinds of proteins accelerate nucleotide hydrolysis by G proteins?
a) guanine nucleotide exchange factor
b) GTPase accelerating protein
c) nuclear localization signal proteins
d) nucleoproins - answer GTPase accelerating protein
In two-dimensional gel electrophoresis, proteins are first resolved by...
and then by...
a) isoelectric focusing; SDS-PAGE
b) SDA-PAGE; affinity chromatography
c) SDS-PAGE; ion exchange
Multiple Choice,
MIP 616 test 1,
MIP616 Exam 1
with 100%
correct answers
already graded
A+(VERIFIED &
UPDATED)
Amino acid in polypeptides are covalently bound by what type of bond?
a) Peptide
b) protein
c) ester
,d) phosphodiester - answer peptide
An alpha helix is what kind of protein structure?
a) secondary
b) primary
c) tertiary
d) quaternary - answer secondary
If you disrupt all hydrogen bonds in a protein, what level will preserved?
a) secondary
b) primary
c) tertiary
d) quaternary - answer primary
Monomeric proteins do not contain a...
a) secondary
b) primary
c) tertiary
d) quaternary - answer quaternary
Which is not part of a zinc finger motif?
a) zinc ion
b) proline residue
c) cysteine residue
d) histidine residue - answer proline residue
a small molecule that binds directly to the active site of an enzyme and
disrupts its catalytic reaction is called:
a) an allosteric inhibitor
b) a competitive inhibitor
,c) a noncompetitive inhibitor
d) RNAi - answer a competitive inhibitor
Which statement about enzymes is TRUE?
a) The catalytic site is responsible for substrate specificity.
b) Reactions catalyzed by enzymes give the products more free energy
than reactions that occur spontaneously.
c) The rate of an enzymatic reaction is always proportional to the
concentration of the substrate
d) Enzymes increase reaction rates by lowering the activation energy
needed to reach the transition state? - answer Enzymes increase reaction
rates by lowering the activation energy needed to reach the transition
state?
Which modification marks a protein for degradation in proteasomes?
a) Phosphorylation
b) Ubiquitinoylation
c) acetylation
d) glycosylation - answer ubiquitinoylation
Kinases activates or inactivate many proteins by doing what to them?
a) methylate
b) phosphorylate
c) acetylate
d) digest - answer phosphorylate
The conversation if inactive chymoptrypsinogen to active chymotryosin is
an example of?
a) proteolytic activation
b) positive cooperativity
c) allostery
d) Ligand induced activation - answer proteolytic activation
, Which amino acid can be phosphorylated?
a) lysine
b) serine
c) glycine
d) proline - answer serine
G proteins act as...
a) a catch
b) a branch
c) a switch
d) a notch - answer a switch
what do g proteins do to their bound nucleotide triphosphate?
a) nebulize it
b) hydrolyze it
c) customize it
d) homogenize it - answer hydrolyze it
What kinds of proteins accelerate nucleotide hydrolysis by G proteins?
a) guanine nucleotide exchange factor
b) GTPase accelerating protein
c) nuclear localization signal proteins
d) nucleoproins - answer GTPase accelerating protein
In two-dimensional gel electrophoresis, proteins are first resolved by...
and then by...
a) isoelectric focusing; SDS-PAGE
b) SDA-PAGE; affinity chromatography
c) SDS-PAGE; ion exchange
