The reason why it makes biochemical sense that chaperones recognize hydrophobic surface area and the catastrophic events are chaperones meant to prevent in cells. Introduction: Molecular chaperones are proteins that help in folding of other proteins to their native structure. The main role of chaperon is to make native folds in proteins, protection of protein subunits from heat shock and prevention of protein from forming aggregation during the assembly of complexes. Hydrophobic areas are exposed in an unfolded protein, making chaperones to bind to these protein areas to assess their folding. Protein structure distortion, protein degradation and their aggregation in the cells are prevented by the chaperones.

Question

Want to see the full answer?

Answer 1

Question

Chapter 6, Problem 20P

Interpretation Introduction

Interpretation:

The reason why it makes biochemical sense that chaperones recognize hydrophobic surface area and the catastrophic events are chaperones meant to prevent in cells.

Introduction:

Molecular chaperones are proteins that help in folding of other proteins to their native structure. The main role of chaperon is to make native folds in proteins, protection of protein subunits from heat shock and prevention of protein from forming aggregation during the assembly of complexes.

Hydrophobic areas are exposed in an unfolded protein, making chaperones to bind to these protein areas to assess their folding. Protein structure distortion, protein degradation and their aggregation in the cells are prevented by the chaperones.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 2

Question

Chapter 6, Problem 20P

Interpretation Introduction

Interpretation:

The reason why it makes biochemical sense that chaperones recognize hydrophobic surface area and the catastrophic events are chaperones meant to prevent in cells.

Introduction:

Molecular chaperones are proteins that help in folding of other proteins to their native structure. The main role of chaperon is to make native folds in proteins, protection of protein subunits from heat shock and prevention of protein from forming aggregation during the assembly of complexes.

Hydrophobic areas are exposed in an unfolded protein, making chaperones to bind to these protein areas to assess their folding. Protein structure distortion, protein degradation and their aggregation in the cells are prevented by the chaperones.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 3

Question

Chapter 6, Problem 20P

Interpretation Introduction

Interpretation:

The reason why it makes biochemical sense that chaperones recognize hydrophobic surface area and the catastrophic events are chaperones meant to prevent in cells.

Introduction:

Molecular chaperones are proteins that help in folding of other proteins to their native structure. The main role of chaperon is to make native folds in proteins, protection of protein subunits from heat shock and prevention of protein from forming aggregation during the assembly of complexes.

Hydrophobic areas are exposed in an unfolded protein, making chaperones to bind to these protein areas to assess their folding. Protein structure distortion, protein degradation and their aggregation in the cells are prevented by the chaperones.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 4

Question

Chapter 6, Problem 20P

Interpretation Introduction

Interpretation:

The reason why it makes biochemical sense that chaperones recognize hydrophobic surface area and the catastrophic events are chaperones meant to prevent in cells.

Introduction:

Molecular chaperones are proteins that help in folding of other proteins to their native structure. The main role of chaperon is to make native folds in proteins, protection of protein subunits from heat shock and prevention of protein from forming aggregation during the assembly of complexes.

Hydrophobic areas are exposed in an unfolded protein, making chaperones to bind to these protein areas to assess their folding. Protein structure distortion, protein degradation and their aggregation in the cells are prevented by the chaperones.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 5

Chapter 6, Problem 20P

Interpretation Introduction

Interpretation:

The reason why it makes biochemical sense that chaperones recognize hydrophobic surface area and the catastrophic events are chaperones meant to prevent in cells.

Introduction:

Molecular chaperones are proteins that help in folding of other proteins to their native structure. The main role of chaperon is to make native folds in proteins, protection of protein subunits from heat shock and prevention of protein from forming aggregation during the assembly of complexes.

Hydrophobic areas are exposed in an unfolded protein, making chaperones to bind to these protein areas to assess their folding. Protein structure distortion, protein degradation and their aggregation in the cells are prevented by the chaperones.

Answer 6

Chapter 6, Problem 20P

Interpretation Introduction

Interpretation:

The reason why it makes biochemical sense that chaperones recognize hydrophobic surface area and the catastrophic events are chaperones meant to prevent in cells.

Introduction:

Molecular chaperones are proteins that help in folding of other proteins to their native structure. The main role of chaperon is to make native folds in proteins, protection of protein subunits from heat shock and prevention of protein from forming aggregation during the assembly of complexes.

Hydrophobic areas are exposed in an unfolded protein, making chaperones to bind to these protein areas to assess their folding. Protein structure distortion, protein degradation and their aggregation in the cells are prevented by the chaperones.

Answer 7

Chapter 6, Problem 20P

Interpretation Introduction

Interpretation:

The reason why it makes biochemical sense that chaperones recognize hydrophobic surface area and the catastrophic events are chaperones meant to prevent in cells.

Introduction:

Molecular chaperones are proteins that help in folding of other proteins to their native structure. The main role of chaperon is to make native folds in proteins, protection of protein subunits from heat shock and prevention of protein from forming aggregation during the assembly of complexes.

Hydrophobic areas are exposed in an unfolded protein, making chaperones to bind to these protein areas to assess their folding. Protein structure distortion, protein degradation and their aggregation in the cells are prevented by the chaperones.

Answer 8

Expert Solution & Answer

Answer 9

Expert Solution & Answer

Answer 10

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 11

Ch. 6 - Prob. 1P Ch. 6 - Bovine pancreatic trypsin inhibitor (BPTI; Figure...Ch. 6 - A schematic structure of the subunit of...Ch. 6 - In the protein adenylate kinase, the C-terminal...Ch. 6 - Give two reasons to explain why a proline residue...Ch. 6 - Consider a small protein containing 101 amino acid...Ch. 6 - a. Based on a more conservative answer to Problem...Ch. 6 - The following sequence is part of a globular...Ch. 6 - a. A protein is found to be a tetramer of...Ch. 6 - Under physiological conditions, the protein...

Concept explainers

Want to see the full answer?

Chapter 6 Solutions