There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O 2 -binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O 2 , and so the Fe atoms must be forced apart when O 2 is bound. Is this molecule likely to show cooperative oxygen binding? Is this molecule likely to exhibit a Bohr Effect? Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue Concept introduction: When O 2 binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism. The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.

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Answer 1

Question

Chapter 7, Problem 12P

Interpretation Introduction

Interpretation:

There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O₂-binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O₂, and so the Fe atoms must be forced apart when O₂ is bound.

Is this molecule likely to show cooperative oxygen binding?

Is this molecule likely to exhibit a Bohr Effect?

Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue

Concept introduction:

When O₂ binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism.

The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.

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Answer 2

Question

Chapter 7, Problem 12P

Interpretation Introduction

Interpretation:

There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O₂-binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O₂, and so the Fe atoms must be forced apart when O₂ is bound.

Is this molecule likely to show cooperative oxygen binding?

Is this molecule likely to exhibit a Bohr Effect?

Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue

Concept introduction:

When O₂ binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism.

The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.

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Answer 3

Question

Chapter 7, Problem 12P

Interpretation Introduction

Interpretation:

There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O₂-binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O₂, and so the Fe atoms must be forced apart when O₂ is bound.

Is this molecule likely to show cooperative oxygen binding?

Is this molecule likely to exhibit a Bohr Effect?

Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue

Concept introduction:

When O₂ binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism.

The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.

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Answer 4

Question

Chapter 7, Problem 12P

Interpretation Introduction

Interpretation:

There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O₂-binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O₂, and so the Fe atoms must be forced apart when O₂ is bound.

Is this molecule likely to show cooperative oxygen binding?

Is this molecule likely to exhibit a Bohr Effect?

Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue

Concept introduction:

When O₂ binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism.

The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.

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Answer 5

Chapter 7, Problem 12P

Interpretation Introduction

Interpretation:

There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O₂-binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O₂, and so the Fe atoms must be forced apart when O₂ is bound.

Is this molecule likely to show cooperative oxygen binding?

Is this molecule likely to exhibit a Bohr Effect?

Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue

Concept introduction:

When O₂ binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism.

The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.

Answer 6

Chapter 7, Problem 12P

Interpretation Introduction

Interpretation:

There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O₂-binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O₂, and so the Fe atoms must be forced apart when O₂ is bound.

Is this molecule likely to show cooperative oxygen binding?

Is this molecule likely to exhibit a Bohr Effect?

Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue

Concept introduction:

When O₂ binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism.

The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.

Answer 7

Chapter 7, Problem 12P

Interpretation Introduction

Interpretation:

There is a salt bridge between residues histidine 13 and aspartic acid 85. The two monomers of a new oxygen transport protein interact by salt bridges between the C- and N-termini. The O₂-binding site lies between the two iron atoms, which are rigidly linked to helices A and C. In the deoxy form, the space between the iron atoms is too small to hold O₂, and so the Fe atoms must be forced apart when O₂ is bound.

Is this molecule likely to show cooperative oxygen binding?

Is this molecule likely to exhibit a Bohr Effect?

Predict the likely effect of a mutation that replaced aspartic acid 85 by a lysine residue

Concept introduction:

When O₂ binds the oxygen transport protein, there is a transition in the protein structure from the low-affinity state to the high-affinity, relaxed state. Binding of oxygen to protein follows an allosteric mechanism.

The Bohr Effect means increase in the carbon dioxide partial pressure of blood or decreases in blood pH results in a lower affinity of hemoglobin for oxygen. This also results in enhanced unloading of oxygen by hemoglobin.

Answer 8

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Answer 10

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Answer 11

Ch. 7 - Prob. 1P Ch. 7 - Certain antibodies have been shown to bind only to...Ch. 7 - Antibodies raised against a macromolecular antigen...Ch. 7 - Prob. 4P Ch. 7 - Prob. 5P Ch. 7 - Prob. 6P Ch. 7 - Prob. 7P Ch. 7 - Prob. 8P Ch. 7 - Prob. 9P Ch. 7 - Prob. 10P

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