The observation that proline residues are never found in short alpha-helices. Introduction: The alpha helix is the common motif within the protein’s secondary structure, and it is the right hand-spiral conformation within which every backbone N-H group gives a hydrogen bond towards a backbone C=O group of an amino acid situated 3 or 4 residues prior along protein sequence.

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Answer 1

Question

Chapter 9, Problem 15P

Interpretation Introduction

To explain:

The observation that proline residues are never found in short alpha-helices.

Introduction:

The alpha helix is the common motif within the protein’s secondary structure, and it is the right hand-spiral conformation within which every backbone N-H group gives a hydrogen bond towards a backbone C=O group of an amino acid situated 3 or 4 residues prior along protein sequence.

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Answer 2

Question

Chapter 9, Problem 15P

Interpretation Introduction

To explain:

The observation that proline residues are never found in short alpha-helices.

Introduction:

The alpha helix is the common motif within the protein’s secondary structure, and it is the right hand-spiral conformation within which every backbone N-H group gives a hydrogen bond towards a backbone C=O group of an amino acid situated 3 or 4 residues prior along protein sequence.

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Answer 3

Question

Chapter 9, Problem 15P

Interpretation Introduction

To explain:

The observation that proline residues are never found in short alpha-helices.

Introduction:

The alpha helix is the common motif within the protein’s secondary structure, and it is the right hand-spiral conformation within which every backbone N-H group gives a hydrogen bond towards a backbone C=O group of an amino acid situated 3 or 4 residues prior along protein sequence.

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Answer 4

Question

Chapter 9, Problem 15P

Interpretation Introduction

To explain:

The observation that proline residues are never found in short alpha-helices.

Introduction:

The alpha helix is the common motif within the protein’s secondary structure, and it is the right hand-spiral conformation within which every backbone N-H group gives a hydrogen bond towards a backbone C=O group of an amino acid situated 3 or 4 residues prior along protein sequence.

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Answer 5

Chapter 9, Problem 15P

Interpretation Introduction

To explain:

The observation that proline residues are never found in short alpha-helices.

Introduction:

The alpha helix is the common motif within the protein’s secondary structure, and it is the right hand-spiral conformation within which every backbone N-H group gives a hydrogen bond towards a backbone C=O group of an amino acid situated 3 or 4 residues prior along protein sequence.

Answer 6

Chapter 9, Problem 15P

Interpretation Introduction

To explain:

The observation that proline residues are never found in short alpha-helices.

Introduction:

The alpha helix is the common motif within the protein’s secondary structure, and it is the right hand-spiral conformation within which every backbone N-H group gives a hydrogen bond towards a backbone C=O group of an amino acid situated 3 or 4 residues prior along protein sequence.

Answer 7

Chapter 9, Problem 15P

Interpretation Introduction

To explain:

The observation that proline residues are never found in short alpha-helices.

Introduction:

The alpha helix is the common motif within the protein’s secondary structure, and it is the right hand-spiral conformation within which every backbone N-H group gives a hydrogen bond towards a backbone C=O group of an amino acid situated 3 or 4 residues prior along protein sequence.

Answer 8

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Answer 9

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Answer 11

Solution Summary: The author explains that proline residues are never found in short alpha-helices.

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