BIOC 384 D2Q-03 QUESTIONS &
ANSWERS 2026 LATEST UPDATE
c. its hydrophobic residues are largely buried in the protein interior - ANSWERA protein
in solution is more likely to maintain its native conformation when______________.
a. the shell of water becomes more ordered
b. the protein is least stable
c. its hydrophobic residues are largely buried in the protein interior
d. the number of hydrogen bonds within a protein is minimized
a. An extended conformation of the polypeptide chain
b. Stabilized by H-bonds between -NH and -CO groups
d. Found in globular proteins
e. The stability is affected by amino acid sequence - ANSWERWhich FOUR statements
are true regarding β sheets?
a. An extended conformation of the polypeptide chain
b. Stabilized by H-bonds between -NH and -CO groups
c. Found in same percentage in all proteins
d. Found in globular proteins
e. The stability is affected by amino acid sequence
f. Includes all 20 standard amino acids in equal frequencies
g. Hydrophobic interactions are responsible for the primary structure
d. predominantly beta sheet - ANSWERWhat class of protein structures does the
protein shown below fit into?
a. intermixed alpha-helix and beta-sheet
b. predominantly alpha-helical
c. domains of alpha-helix adjacent to domains of beta-sheet
d. predominantly beta sheet
a. disulfide bonding - ANSWERWhich stabilizing force in protein tertiary structures is a
covalent bonding force?
a. disulfide bonding
b. hydrophobic effects
c. ionic bonding
d. van der Waals interactions
a. tyrosine - ANSWERFrom the list below, which amino acid has an uncharged side
chain at pH 7?
, a. tyrosine
b. arginine
c. glutamate
d. aspartate
e. lysine
b. pH 11 - helix
e. pH 7 - random coil
f. pH 1 - random coil - ANSWERA homopolymer of lysine residues (polylysine) can
adopt an alpha-helical conformation or a random coil conformation depending on the pH
of the solution. Predict whether the conformation of polylysine would be a-helical or
random coil at a pH of 1, 7, and 11.
Choose a total of THREE answers. Choose either helix or random coil for pH 1, pH 7,
and pH 11.
a. pH 7 - helix
b. pH 11 - helix
c. pH 1 - helix
d. pH 11 - random coil
e. pH 7 - random coil
f. pH 1 - random coil
e. Removal of β-mercaptoethanol (BME) and urea at the same time allowed for the
unfolded protein to refold. - ANSWERFor Anfinsen's studies of RNase A folding, which
of the following is correct?
a. Urea is a highly polar solvent that can be used to fold proteins through formation of
Intramolecular hydrogen bonds
b. Addition of β-mercaptoethanol and urea at the same time resulted in active RNaseA.
c. Removal of β-mercaptoethanol (BME), followed by raising the temperature to 90ºC,
resulted in active RNaseA.
d. β-mercaptoethanol (BME) was used to disrupt disulfide bonds of the native protein so
refolding could occur under favorable conditions.
e. Removal of β-mercaptoethanol (BME) and urea at the same time allowed for the
unfolded protein to refold.
f. Removal of β-mercaptoethanol (BME) and urea at the same time allowed for the
folded protein to unfold.
g. Trace amounts of urea could be added to inactive protein to rescue the experiment.
a. bind to the hydrophobic residues on the misfolded protein. - ANSWERWhen Hsp70
binds ATP, it undergoes a conformational change that exposes hydrophobic residues.
The exposed hydrophobic residues on Hsp70
a. bind to the hydrophobic residues on the misfolded protein.
b. bind to the hydrophilic residues on the misfolded protein.
ANSWERS 2026 LATEST UPDATE
c. its hydrophobic residues are largely buried in the protein interior - ANSWERA protein
in solution is more likely to maintain its native conformation when______________.
a. the shell of water becomes more ordered
b. the protein is least stable
c. its hydrophobic residues are largely buried in the protein interior
d. the number of hydrogen bonds within a protein is minimized
a. An extended conformation of the polypeptide chain
b. Stabilized by H-bonds between -NH and -CO groups
d. Found in globular proteins
e. The stability is affected by amino acid sequence - ANSWERWhich FOUR statements
are true regarding β sheets?
a. An extended conformation of the polypeptide chain
b. Stabilized by H-bonds between -NH and -CO groups
c. Found in same percentage in all proteins
d. Found in globular proteins
e. The stability is affected by amino acid sequence
f. Includes all 20 standard amino acids in equal frequencies
g. Hydrophobic interactions are responsible for the primary structure
d. predominantly beta sheet - ANSWERWhat class of protein structures does the
protein shown below fit into?
a. intermixed alpha-helix and beta-sheet
b. predominantly alpha-helical
c. domains of alpha-helix adjacent to domains of beta-sheet
d. predominantly beta sheet
a. disulfide bonding - ANSWERWhich stabilizing force in protein tertiary structures is a
covalent bonding force?
a. disulfide bonding
b. hydrophobic effects
c. ionic bonding
d. van der Waals interactions
a. tyrosine - ANSWERFrom the list below, which amino acid has an uncharged side
chain at pH 7?
, a. tyrosine
b. arginine
c. glutamate
d. aspartate
e. lysine
b. pH 11 - helix
e. pH 7 - random coil
f. pH 1 - random coil - ANSWERA homopolymer of lysine residues (polylysine) can
adopt an alpha-helical conformation or a random coil conformation depending on the pH
of the solution. Predict whether the conformation of polylysine would be a-helical or
random coil at a pH of 1, 7, and 11.
Choose a total of THREE answers. Choose either helix or random coil for pH 1, pH 7,
and pH 11.
a. pH 7 - helix
b. pH 11 - helix
c. pH 1 - helix
d. pH 11 - random coil
e. pH 7 - random coil
f. pH 1 - random coil
e. Removal of β-mercaptoethanol (BME) and urea at the same time allowed for the
unfolded protein to refold. - ANSWERFor Anfinsen's studies of RNase A folding, which
of the following is correct?
a. Urea is a highly polar solvent that can be used to fold proteins through formation of
Intramolecular hydrogen bonds
b. Addition of β-mercaptoethanol and urea at the same time resulted in active RNaseA.
c. Removal of β-mercaptoethanol (BME), followed by raising the temperature to 90ºC,
resulted in active RNaseA.
d. β-mercaptoethanol (BME) was used to disrupt disulfide bonds of the native protein so
refolding could occur under favorable conditions.
e. Removal of β-mercaptoethanol (BME) and urea at the same time allowed for the
unfolded protein to refold.
f. Removal of β-mercaptoethanol (BME) and urea at the same time allowed for the
folded protein to unfold.
g. Trace amounts of urea could be added to inactive protein to rescue the experiment.
a. bind to the hydrophobic residues on the misfolded protein. - ANSWERWhen Hsp70
binds ATP, it undergoes a conformational change that exposes hydrophobic residues.
The exposed hydrophobic residues on Hsp70
a. bind to the hydrophobic residues on the misfolded protein.
b. bind to the hydrophilic residues on the misfolded protein.
