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BCCB2000 Lecture 6 Questions Exam Latest Update
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BCCB2000 Lecture 6 QuestionsExam Latest Update
Which of the following is not correct concerning 2,3-bisphosphoglycerate (BPG)?
A. It increases the affinity of hemoglobin for oxygen.
B. It binds at a distance from the heme groups of hemoglobin.
C. It is normally found associated with the hemoglobin molecules that are extracted
from red blood cells.
D. It is an allosteric modulator.
E. It binds with lower affinity to fetal hemoglobin than to adult hemoglobin. - Answer A. It
increases the affinity of hemoglobin for oxygen.
Cooperative binding of oxygen by hemoglobin:
A. is induced by hemoglobin.
B. is a result of different affinities for oxygen by each subunit protein.
C. is induced by oxygenation.
D. is a result of interaction with myoglobin. - Answer C. is induced by oxygenation.
An allosteric interaction between a ligand and a protein is one in which:
A. two different ligands can bind to the same binding site.
B. the binding of the ligand to the protein is covalent
C. multiple molecules of the same ligand can bind to the same binding site
D. the binding of a molecule to a binding site affects the binding of an additional
molecule to the same site
E. the binding of a molecule to a binding site affects the binding properties of another
site on the protein - Answer E. the binding of a molecule to a binding site affects the
binding properties of another site on the protein
Haemoglobin is:
A. a tetramer of 4 myoglobin proteins.
B. a tetramer of four globin chains and one heme prosthetic group.
, C. a dimer of subunits each with two distinct protein chains (alpha and beta).
D. a dimer of subunits each with two myoglobin proteins.
E. an erythrocyte. - Answer C. a dimer of subunits each with two distinct protein chains
(alpha and beta).
A hyperbolic binding curve differs from a sigmoidal binding curve in that the hyperbolic
curve:
A. has a single equilibrium constant for oxygen binding.
B. binds more oxygen after the initial proteins first bind oxygen.
C. shows cooperativity.
D. binds up to four molecules of oxygen.
E. All of the above - Answer A. has a single equilibrium constant for oxygen binding.
The role of the proximal histidine in myoglobin is to:
A. prevent tight CO binding
B. bind to the fifth coordination position of Fe2+
C. bind H2O
D. bind O2
E. prevent tight CO2 binding - Answer B. bind to the fifth coordination position of Fe2+
Haemoglobin has the following roles in vertebrates:
A. transports oxygen
B. transports CO2
C. transports H+
D. acts as a buffer
E. all of the above - Answer E. all of the above
Which statement is false about the heme group?
A. When oxygen binds to heme, the iron ion is oxidized from Fe2+ to Fe3+.
B. If exposed to air, a free heme group (not associated with hemoglobin) is readily
oxidized converting Fe2+ to Fe3+ and can no longer bind oxygen.
C. The heme group is tightly, but non-covalently, held in myoglobin molecule.
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