Question 1

What is the Bohr effect?

Accepted Answer

A)  the ability of hemoglobin to retain oxygen when in competition with myoglobin 
B)  the regulation of hemoglobin binding by hydrogen ions and carbon dioxide 
C)  the alteration of hemoglobin conformation during low-oxygen stress 
D)  All of the above. 
E)  None of the above. 
A)  the ability of hemoglobin to retain oxygen when in competition with myoglobin 
B)  the regulation of hemoglobin binding by hydrogen ions and carbon dioxide 
C)  the alteration of hemoglobin conformation during low-oxygen stress 
D)  All of the above. 
E)  None of the above.

Question 2

What factor(s) influence(s) the binding of oxygen to myoglobin?

Accepted Answer

A)  the concentration of bicarbonate ion, HCO3− 
B)  the partial pressure of oxygen, pO2 
C)  the concentration of hemoglobin present 
D)  the concentration of 2,3-BPG 
E)  B and D 
A)  the concentration of bicarbonate ion, HCO3− 
B)  the partial pressure of oxygen, pO2 
C)  the concentration of hemoglobin present 
D)  the concentration of 2,3-BPG 
E)  B and D

Question 3

Which of the following is correct concerning the following equilibria? CO2 + H2O↔H2CO3

Accepted Answer

A)  An increase in the pressure of CO2 will result in a decrease of pH. 
B)  This reaction is catalyzed by carbonic anhydrase. 
C)  The H2CO3 dissociates to H+ and bicarbonate ion, HCO3−. 
D)  The majority of CO2 is transported to the lungs in the form of HCO3−. 
E)  All of the above. 
A)  An increase in the pressure of CO2 will result in a decrease of pH. 
B)  This reaction is catalyzed by carbonic anhydrase. 
C)  The H2CO3 dissociates to H+ and bicarbonate ion, HCO3−. 
D)  The majority of CO2 is transported to the lungs in the form of HCO3−. 
E)  All of the above.

Question 4

Which of the following is correct concerning fetal hemoglobin?

Accepted Answer

A)  Fetal hemoglobin is composed of two α and two γ subunits. 
B)  Fetal hemoglobin binds 2,3-BPG more tightly than normal adult hemoglobin. 
C)  Fetal hemoglobin binds oxygen less than HbA at all pO2. 
D)  Fetal hemoglobin does not exist in the T form. 
E)  None of the above. 
A)  Fetal hemoglobin is composed of two α and two γ subunits. 
B)  Fetal hemoglobin binds 2,3-BPG more tightly than normal adult hemoglobin. 
C)  Fetal hemoglobin binds oxygen less than HbA at all pO2. 
D)  Fetal hemoglobin does not exist in the T form. 
E)  None of the above.

Question 5

Describe the structure of normal adult hemoglobin.

Accepted Answer

Normal adult hemoglobin, HbA, is a tetra

Question 6

Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The type of binding that is indicated by a sigmoidal-shaped binding curve.

Accepted Answer

A) cooperative 
B) oxygen 
C) fMRI 
D) carbamate 
E) histidine
F)hyperbolic
G)myoglobin
H)bicarbonate ion
I)sickle-cell anemia
J)protoporphyrin
K)fetal
L)carbonic acid 
A) cooperative 
B) oxygen 
C) fMRI 
D) carbamate 
E) histidine
F)hyperbolic
G)myoglobin
H)bicarbonate ion
I)sickle-cell anemia
J)protoporphyrin
K)fetal
L)carbonic acid

Question 7

Why is it advantageous for hemoglobin to have allosteric properties?

Accepted Answer

Hemoglobin binds oxygen in a positive co

Question 8

Briefly describe cooperative binding.

Accepted Answer

Cooperative binding occurs in multi-subu

Question 9

Briefly describe the cause of sickle-cell anemia.

Accepted Answer

Sickle-cell anemia is a genetic disorder

Question 10

Describe the chemical basis of the Bohr effect.

Accepted Answer

The effect observed by Christian Bohr is

Question 11

Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The substance produced when carbon dioxide reacts with water.

Accepted Answer

A) cooperative 
B) oxygen 
C) fMRI 
D) carbamate 
E) histidine
F)hyperbolic
G)myoglobin
H)bicarbonate ion
I)sickle-cell anemia
J)protoporphyrin
K)fetal
L)carbonic acid 
A) cooperative 
B) oxygen 
C) fMRI 
D) carbamate 
E) histidine
F)hyperbolic
G)myoglobin
H)bicarbonate ion
I)sickle-cell anemia
J)protoporphyrin
K)fetal
L)carbonic acid

Question 12

Choose the correct answer from the list below. Not all of the answers will be used.
-____________: This condition is a result of a single point mutation in the β chain of hemoglobin.

Accepted Answer

A) cooperative 
B) oxygen 
C) fMRI 
D) carbamate 
E) histidine
F)hyperbolic
G)myoglobin
H)bicarbonate ion
I)sickle-cell anemia
J)protoporphyrin
K)fetal
L)carbonic acid 
A) cooperative 
B) oxygen 
C) fMRI 
D) carbamate 
E) histidine
F)hyperbolic
G)myoglobin
H)bicarbonate ion
I)sickle-cell anemia
J)protoporphyrin
K)fetal
L)carbonic acid

Question 13

2,3-bisphosphoglycerate binds only to the _____________ form of hemoglobin.

Accepted Answer

The answer of 2,3-bisphosphoglycerate binds only to the _____________ form...

Question 14

The T state of hemoglobin is stabilized by a salt bridge between β1 Asp 94 and the C-terminal _____________ of the β1 chain.

Accepted Answer

Question 15

In normal adult hemoglobin, HbA, the β6 position is a glutamate residue, whereas in sickle-cell hemoglobin, HbS, it is a(n) _____________ residue.

Accepted Answer

The answer of In normal adult hemoglobin, HbA, the β6...

Question 16

Describe the concerted model to explain allosteric cooperative binding

Accepted Answer

The protein exists in two conformations,

Question 17

As the partial pressure of carbon dioxide increases, the affinity of oxygen binding to hemoglobin _____________.

Accepted Answer

The answer of As the partial pressure of carbon dioxide...

Question 18

What is fetal hemoglobin? How does it differ from adult hemoglobin?

Accepted Answer

Fetal hemoglobin contains two ɑ and two

Question 19

The binding of 2,3-bisphosphoglycerate to hemoglobin _____________ (increases, decreases) its affinity of oxygen binding.

Accepted Answer

The answer of The binding of 2,3-bisphosphoglycerate to hemoglobin _____________...

Question 20

Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The organic portion of the heme group in hemoglobin.

Accepted Answer

A) cooperative 
B) oxygen 
C) fMRI 
D) carbamate 
E) histidine
F)hyperbolic
G)myoglobin
H)bicarbonate ion
I)sickle-cell anemia
J)protoporphyrin
K)fetal
L)carbonic acid 
A) cooperative 
B) oxygen 
C) fMRI 
D) carbamate 
E) histidine
F)hyperbolic
G)myoglobin
H)bicarbonate ion
I)sickle-cell anemia
J)protoporphyrin
K)fetal
L)carbonic acid

Exam 9: Hemoglobin: an Allosteric Protein

What is the Bohr effect?

What factor(s) influence(s) the binding of oxygen to myoglobin?

Which of the following is correct concerning the following equilibria? CO2 + H2O↔H2CO3

Which of the following is correct concerning fetal hemoglobin?

Describe the structure of normal adult hemoglobin.

Choose the correct answer from the list below. Not all of the answers will be used. -____________: The type of binding that is indicated by a sigmoidal-shaped binding curve.

Why is it advantageous for hemoglobin to have allosteric properties?

Briefly describe cooperative binding.

Briefly describe the cause of sickle-cell anemia.

Describe the chemical basis of the Bohr effect.

Choose the correct answer from the list below. Not all of the answers will be used. -____________: The substance produced when carbon dioxide reacts with water.

Choose the correct answer from the list below. Not all of the answers will be used. -____________: This condition is a result of a single point mutation in the β chain of hemoglobin.

2,3-bisphosphoglycerate binds only to the _____________ form of hemoglobin.

The T state of hemoglobin is stabilized by a salt bridge between β1 Asp 94 and the C-terminal _____________ of the β1 chain.

In normal adult hemoglobin, HbA, the β6 position is a glutamate residue, whereas in sickle-cell hemoglobin, HbS, it is a(n) _____________ residue.

Describe the concerted model to explain allosteric cooperative binding

As the partial pressure of carbon dioxide increases, the affinity of oxygen binding to hemoglobin _____________.

What is fetal hemoglobin? How does it differ from adult hemoglobin?

The binding of 2,3-bisphosphoglycerate to hemoglobin _____________ (increases, decreases) its affinity of oxygen binding.

Choose the correct answer from the list below. Not all of the answers will be used. -____________: The organic portion of the heme group in hemoglobin.

Biochemistry and the Unity of Life

Water, Weak Bonds, and the Generation of Order Out of Chaos

Amino Acids

Protein Three-Dimensional Structure

Techniques in Protein Biochemistry

Basic Concepts of Enzyme Action

Kinetics and Regulation

Mechanisms and Inhibitors

Carbohydrates

Lipids

Membrane Structure and Function

Signal Transduction Pathways

Digestion: Turning a Meal Into Cellular Biochemicals

Metabolism: Basic Concepts and Design

Glycolysis

Gluconeogenesis

Preparation for the Cycle

Harvesting Electrons From the Cycle

The Electron Transport Chain

The Proton-Motive Force

The Light Reactions

The Calvin Cycle

Glycogen Degradation

Glycogen Synthesis

The Pentose Phosphate Pathway

Fatty Acid Degredation

Fatty Acid Synthesis

Lipid Synthesis

Amino Acid Degradation and the Urea Cycle

Amino Acids Synthesis

Nucleotide Metabolism

The Structure of Informational Macromolecules: Dna and Rna

DNA Replication

DNA Repair and Recombination

RNA Synthesis and Regulation in Prokaryotes

Gene Expression in Eukaryotes

RNA Processing in Eukaryotes

The Genetic Code

The Mechanism of Protein Synthesis

Recombinant DNA Techniques

Filters

Which of the following is correct concerning the following equilibria? CO₂ + H₂O↔H₂CO₃

The T state of hemoglobin is stabilized by a salt bridge between β₁ Asp 94 and the C-terminal _____________ of the β₁ chain.