BCH 403 Final Exam with Questions Solved
100% Correct | Latest Update
E1: Why do proteins fold? - Answer A and B are correct (It is entropically favorable for
water & It is enthalpically favorable for the protein)
E1: The structural changes in hemoglobin that contribute toward its positive
cooperativity for oxygen consist of: - Answer All of the above ( movement of iron into
the plane of the heme & movement of a neighboring veiling residue due to strain from
changes in the heme & the breaking of a covalent bond with the regulatory molecule
BPG
E1: The following oxygen binding curves are derived from independent experiments.
which of the following statements is not true regarding these plots?
[Plot picture may insert later] - Answer when comparing 3 with 4 comma careforce less
likely to be bound to BPG
E1: What is the molecular basis for sickle cell anemia? - Answer A polar surface residue
in hemoglobin is mutated to valine, a nonpolar residue, causing the protein to aggregate
into fibers
E1: Which of the following tripeptides will bind to an anion exchange column at pH 7
Peptide A: Glu-Lys-Arg Peptide B: Glu-Asp-Arg - Answer Peptide B will bond
E1: Which of the following is true regarding Michaelis-Menton enzyme kinetics? -
Answer B and C are correct (the Michaelis constant (KM) is the substrate concentration
,when the velocity is one half of maximum & at infinite substrate concentration, the
reaction becomes zero order with respect to substrate)
E1: In an enzyme catalyzed reaction, the Delta Delta G naught ++ ( change in the free
energy of activation) is found to be very small when compared to the net free energy of
activation. Which of the following are also true of this reaction? - Answer The velocity
will increase slightly.
E1: A biochemical reaction, without a catalyst or thermodynamic coupling, takes 50
years to reach a state of equilibrium. Without more information, we cannot make a
determination on either the value of Keq constant or the positive or negative value of
the deltaG of the reaction. - Answer FALSE
E1: Due to its small size, the amino acid glycine can be found in tight turns in a protein
structure - Answer TRUE
E1: The deltaG of a reaction is defined as the energy required to bring the concentration
of the reactants and products to equal concentration. - Answer FALSE
E1: One strength of nuclear magnetic resonance spectroscopy is that it can detect
multiple conformations of proteins and one of its limitations is that proteins must
contain certain isotopes. - Answer TRUE
E1: A single residue mutation to an enzyme decreases its rate constant by one half. This
means the reaction now occurs more slowly. - Answer TRUE
The hydrophobic packing of non-polar residues is thermodynamically favorable because
of both the hydrophobic effect and a larger number of weak van der Waals interactions.
- Answer TRUE
, E1: The classic experiment in which the protein ribonuclease A is first denatured and
reduced, then refolded, was used to demonstrate the role of aromatic residues in
stabilizing covalent disulfide bonds. - Answer FALSE
E1: One reason that we require myoglobin and hemoglobin to store and transport
oxygen is because oxygen by itself has very poor solubility in water - Answer TRUE
E1: A mutation in myoglobin that changes the distal histidine to an alanine will result in
a lower P50 - Answer FALSE
E1: The stabililty of an a-helix is partly due to the hydrogen bonding that occurs
between the carbonyl oxygen of one helix and the amide hydrogen of a neighboring a-
helix - Answer FALSE
E1: Which of the following statements is true regarding the hydrophobic effect? -
Answer Non - Polar molecules are driven together in order to maximize the entropy of
water.
E1: The peptide in question 17 is dissolved into a solution that has a pH of 6.5. Under
these conditions the net charge of the peptide is - Answer +1
E1: A glycine residue is disruptive to the stability of an a-helix or a b-strand because: -
Answer It's R-group is too small to participate in stabilizing interactions with neighboring
R - groups
E1: With a pKa of 6.37 the carbonic acid/bicarbonate system serves to buffer changes to
the pH of blood. The acid dissociates as follows:
H2CO3 + H20 <-> HCO3- + H30+
100% Correct | Latest Update
E1: Why do proteins fold? - Answer A and B are correct (It is entropically favorable for
water & It is enthalpically favorable for the protein)
E1: The structural changes in hemoglobin that contribute toward its positive
cooperativity for oxygen consist of: - Answer All of the above ( movement of iron into
the plane of the heme & movement of a neighboring veiling residue due to strain from
changes in the heme & the breaking of a covalent bond with the regulatory molecule
BPG
E1: The following oxygen binding curves are derived from independent experiments.
which of the following statements is not true regarding these plots?
[Plot picture may insert later] - Answer when comparing 3 with 4 comma careforce less
likely to be bound to BPG
E1: What is the molecular basis for sickle cell anemia? - Answer A polar surface residue
in hemoglobin is mutated to valine, a nonpolar residue, causing the protein to aggregate
into fibers
E1: Which of the following tripeptides will bind to an anion exchange column at pH 7
Peptide A: Glu-Lys-Arg Peptide B: Glu-Asp-Arg - Answer Peptide B will bond
E1: Which of the following is true regarding Michaelis-Menton enzyme kinetics? -
Answer B and C are correct (the Michaelis constant (KM) is the substrate concentration
,when the velocity is one half of maximum & at infinite substrate concentration, the
reaction becomes zero order with respect to substrate)
E1: In an enzyme catalyzed reaction, the Delta Delta G naught ++ ( change in the free
energy of activation) is found to be very small when compared to the net free energy of
activation. Which of the following are also true of this reaction? - Answer The velocity
will increase slightly.
E1: A biochemical reaction, without a catalyst or thermodynamic coupling, takes 50
years to reach a state of equilibrium. Without more information, we cannot make a
determination on either the value of Keq constant or the positive or negative value of
the deltaG of the reaction. - Answer FALSE
E1: Due to its small size, the amino acid glycine can be found in tight turns in a protein
structure - Answer TRUE
E1: The deltaG of a reaction is defined as the energy required to bring the concentration
of the reactants and products to equal concentration. - Answer FALSE
E1: One strength of nuclear magnetic resonance spectroscopy is that it can detect
multiple conformations of proteins and one of its limitations is that proteins must
contain certain isotopes. - Answer TRUE
E1: A single residue mutation to an enzyme decreases its rate constant by one half. This
means the reaction now occurs more slowly. - Answer TRUE
The hydrophobic packing of non-polar residues is thermodynamically favorable because
of both the hydrophobic effect and a larger number of weak van der Waals interactions.
- Answer TRUE
, E1: The classic experiment in which the protein ribonuclease A is first denatured and
reduced, then refolded, was used to demonstrate the role of aromatic residues in
stabilizing covalent disulfide bonds. - Answer FALSE
E1: One reason that we require myoglobin and hemoglobin to store and transport
oxygen is because oxygen by itself has very poor solubility in water - Answer TRUE
E1: A mutation in myoglobin that changes the distal histidine to an alanine will result in
a lower P50 - Answer FALSE
E1: The stabililty of an a-helix is partly due to the hydrogen bonding that occurs
between the carbonyl oxygen of one helix and the amide hydrogen of a neighboring a-
helix - Answer FALSE
E1: Which of the following statements is true regarding the hydrophobic effect? -
Answer Non - Polar molecules are driven together in order to maximize the entropy of
water.
E1: The peptide in question 17 is dissolved into a solution that has a pH of 6.5. Under
these conditions the net charge of the peptide is - Answer +1
E1: A glycine residue is disruptive to the stability of an a-helix or a b-strand because: -
Answer It's R-group is too small to participate in stabilizing interactions with neighboring
R - groups
E1: With a pKa of 6.37 the carbonic acid/bicarbonate system serves to buffer changes to
the pH of blood. The acid dissociates as follows:
H2CO3 + H20 <-> HCO3- + H30+
