The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape. Introduction: The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

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Chapter 3, Problem 6TYU

Summary Introduction

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

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The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in the solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface do. Determination of these rates can be used to explore the proteinfolding reaction, probe the tertiary structure of proteins, and identify the regions of protein–protein interfaces. These exchange reactions can be followed by studying the behavior of the protein in solvent that has been labeled with deuterium ( ²H), a stable isotope of hydrogen. What two methods described in this chapter could be readily applied to the study of hydrogen– deuterium exchange rates in proteins?

Which of the following statements are true? Electrostatic interactions are the dominant forces in protein molecular recognition. When two proteins form a complex there is an unfavorable loss of rotational-translational entropy. Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy. The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins. Burial of an uncompensated positive charge inside proteins is usually unfavorable. So-called van der Waals’ interactions are essentially electrostatic in origin. Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding. Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.

list other biological examples in which specific protein interactions are involved.

Answer 2

Question

Chapter 3, Problem 6TYU

Summary Introduction

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

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Answer 3

Question

Chapter 3, Problem 6TYU

Summary Introduction

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

Expert Solution & Answer

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Answer 4

Question

Chapter 3, Problem 6TYU

Summary Introduction

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

Expert Solution & Answer

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Answer 5

Chapter 3, Problem 6TYU

Summary Introduction

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

Answer 6

Chapter 3, Problem 6TYU

Summary Introduction

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

Answer 7

Chapter 3, Problem 6TYU

Summary Introduction

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

Answer 8

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Answer 11

Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - 2. What type of bond is directly involved in the...Ch. 3 - What type of information is used to direct...Ch. 3 - 4. What is an active site? a. the location in an...Ch. 3 - Prob. 5TYU Ch. 3 - Prob. 6TYU Ch. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 8TYU Ch. 3 - Prob. 9TYPSS Ch. 3 - 10. Make a concept map (see BioSkills 12) that...

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape. Introduction: The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

Solution Summary: The author describes the mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Concept explainers

Videos

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

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Chapter 3 Solutions

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape. Introduction: The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

Solution Summary: The author describes the mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Concept explainers

Videos

To review: The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape. Introduction: The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.

Want to see the full answer?

Chapter 3 Solutions

To review:

The mechanism used by molecular chaperones to facilitate protein folding in many different polypeptides, each with their own specific shape.

Introduction:

The molecular chaperones are a large family of highly conserved proteins that help in covalent folding or unfolding of proteins.