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MIP 616 Exam 1 Questions With Complete
Solutions
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
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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
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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
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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
MIP 616 Exam 1 Questions With Complete
Solutions
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
,2|Page
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
,3|Page
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
, 4|Page
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
