The notation for the α helix. Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. α helix is formed when the peptide bond (C=O) of the nth residue along the helical axis points toward the peptide N-H group of the (n+4)th residue. This forms a strong backbone hydrogen bonds. There are 3.6 residues per turn in the right-handed helical conformation.

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Answer 1

Question

Chapter 6, Problem 21CQ

(a)

Summary Introduction

To identify: The notation for the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. α helix is formed when the peptide bond (C=O) of the nth residue along the helical axis points toward the peptide N-H group of the (n+4)th residue. This forms a strong backbone hydrogen bonds. There are 3.6 residues per turn in the right-handed helical conformation.

(b)

Summary Introduction

To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

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Answer 2

Question

Chapter 6, Problem 21CQ

(a)

Summary Introduction

To identify: The notation for the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. α helix is formed when the peptide bond (C=O) of the nth residue along the helical axis points toward the peptide N-H group of the (n+4)th residue. This forms a strong backbone hydrogen bonds. There are 3.6 residues per turn in the right-handed helical conformation.

(b)

Summary Introduction

To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

Expert Solution & Answer

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Answer 3

Question

Chapter 6, Problem 21CQ

(a)

Summary Introduction

To identify: The notation for the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. α helix is formed when the peptide bond (C=O) of the nth residue along the helical axis points toward the peptide N-H group of the (n+4)th residue. This forms a strong backbone hydrogen bonds. There are 3.6 residues per turn in the right-handed helical conformation.

(b)

Summary Introduction

To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

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Answer 4

Question

Chapter 6, Problem 21CQ

(a)

Summary Introduction

To identify: The notation for the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. α helix is formed when the peptide bond (C=O) of the nth residue along the helical axis points toward the peptide N-H group of the (n+4)th residue. This forms a strong backbone hydrogen bonds. There are 3.6 residues per turn in the right-handed helical conformation.

(b)

Summary Introduction

To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

Expert Solution & Answer

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Answer 5

Chapter 6, Problem 21CQ

(a)

Summary Introduction

To identify: The notation for the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. α helix is formed when the peptide bond (C=O) of the nth residue along the helical axis points toward the peptide N-H group of the (n+4)th residue. This forms a strong backbone hydrogen bonds. There are 3.6 residues per turn in the right-handed helical conformation.

(b)

Summary Introduction

To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

Answer 6

Chapter 6, Problem 21CQ

(a)

Summary Introduction

To identify: The notation for the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. α helix is formed when the peptide bond (C=O) of the nth residue along the helical axis points toward the peptide N-H group of the (n+4)th residue. This forms a strong backbone hydrogen bonds. There are 3.6 residues per turn in the right-handed helical conformation.

Answer 7

Chapter 6, Problem 21CQ

(a)

Summary Introduction

To identify: The notation for the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. α helix is formed when the peptide bond (C=O) of the nth residue along the helical axis points toward the peptide N-H group of the (n+4)th residue. This forms a strong backbone hydrogen bonds. There are 3.6 residues per turn in the right-handed helical conformation.

Answer 8

(b)

Summary Introduction

To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

Answer 9

(b)

Summary Introduction

To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

Answer 10

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Answer 11

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Answer 12

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Answer 13

Ch. 6 - Prob. 1E Ch. 6 - Prob. 2E Ch. 6 - 3. Why would you be unlikely to see an ? helix...Ch. 6 - 4. Calculate the length in angstroms of a...Ch. 6 - Prob. 5E Ch. 6 - 6. Collagen IV, which occurs in basement...Ch. 6 - 7. Describe the primary, secondary, tertiary, and...Ch. 6 - 8. Explain why gelatin, which is mostly collagen,...Ch. 6 - Prob. 9E Ch. 6 - 10. Is it possible for a native protein to be...

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To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

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Chapter 6 Solutions

Concept explainers

Videos

To identify: Whether the 310 helix is steeper or swallower than the α helix. Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.

Want to see the full answer?

Chapter 6 Solutions

To identify: Whether the 3₁₀ helix is steeper or swallower than the α helix.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The amino acids are arranged in a right handed helical structure. It corresponds to 120° turn in the helix.