The reason behind polar or charged residues usually appear in the remaining five positions in the polypeptide chain that form coiled coils Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The 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. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Question

Want to see the full answer?

Answer 1

Question

Chapter 6, Problem 22CQ

(a)

Summary Introduction

To explain: The reason behind polar or charged residues usually appear in the remaining five positions in the polypeptide chain that form coiled coils

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The 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. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

(b)

Summary Introduction

To explain: The reason behind the sequence Ile-Gln-Glu-Val-Glu-Arg-Arp is more likely than the sequence Trp-Gln-Glu-Tyr-Glu-Arg-Asp to appear in a coiled coil.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The residues at the first and fourth side chains of two helices usually form hydrophobic interacting surfaces that are buried in the core. α helix is formed when the peptide bond (C=O) of the nth residue points along the helical axis toward the peptide N-H group of the (n+4)th residue. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 2

Question

Chapter 6, Problem 22CQ

(a)

Summary Introduction

To explain: The reason behind polar or charged residues usually appear in the remaining five positions in the polypeptide chain that form coiled coils

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The 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. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

(b)

Summary Introduction

To explain: The reason behind the sequence Ile-Gln-Glu-Val-Glu-Arg-Arp is more likely than the sequence Trp-Gln-Glu-Tyr-Glu-Arg-Asp to appear in a coiled coil.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The residues at the first and fourth side chains of two helices usually form hydrophobic interacting surfaces that are buried in the core. α helix is formed when the peptide bond (C=O) of the nth residue points along the helical axis toward the peptide N-H group of the (n+4)th residue. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 3

Question

Chapter 6, Problem 22CQ

(a)

Summary Introduction

To explain: The reason behind polar or charged residues usually appear in the remaining five positions in the polypeptide chain that form coiled coils

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The 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. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

(b)

Summary Introduction

To explain: The reason behind the sequence Ile-Gln-Glu-Val-Glu-Arg-Arp is more likely than the sequence Trp-Gln-Glu-Tyr-Glu-Arg-Asp to appear in a coiled coil.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The residues at the first and fourth side chains of two helices usually form hydrophobic interacting surfaces that are buried in the core. α helix is formed when the peptide bond (C=O) of the nth residue points along the helical axis toward the peptide N-H group of the (n+4)th residue. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 4

Question

Chapter 6, Problem 22CQ

(a)

Summary Introduction

To explain: The reason behind polar or charged residues usually appear in the remaining five positions in the polypeptide chain that form coiled coils

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The 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. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

(b)

Summary Introduction

To explain: The reason behind the sequence Ile-Gln-Glu-Val-Glu-Arg-Arp is more likely than the sequence Trp-Gln-Glu-Tyr-Glu-Arg-Asp to appear in a coiled coil.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The residues at the first and fourth side chains of two helices usually form hydrophobic interacting surfaces that are buried in the core. α helix is formed when the peptide bond (C=O) of the nth residue points along the helical axis toward the peptide N-H group of the (n+4)th residue. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Answer 5

Chapter 6, Problem 22CQ

(a)

Summary Introduction

To explain: The reason behind polar or charged residues usually appear in the remaining five positions in the polypeptide chain that form coiled coils

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The 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. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

(b)

Summary Introduction

To explain: The reason behind the sequence Ile-Gln-Glu-Val-Glu-Arg-Arp is more likely than the sequence Trp-Gln-Glu-Tyr-Glu-Arg-Asp to appear in a coiled coil.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The residues at the first and fourth side chains of two helices usually form hydrophobic interacting surfaces that are buried in the core. α helix is formed when the peptide bond (C=O) of the nth residue points along the helical axis toward the peptide N-H group of the (n+4)th residue. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Answer 6

Chapter 6, Problem 22CQ

(a)

Summary Introduction

To explain: The reason behind polar or charged residues usually appear in the remaining five positions in the polypeptide chain that form coiled coils

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The 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. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Answer 7

Chapter 6, Problem 22CQ

(a)

Summary Introduction

To explain: The reason behind polar or charged residues usually appear in the remaining five positions in the polypeptide chain that form coiled coils

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The 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. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Answer 8

(b)

Summary Introduction

To explain: The reason behind the sequence Ile-Gln-Glu-Val-Glu-Arg-Arp is more likely than the sequence Trp-Gln-Glu-Tyr-Glu-Arg-Asp to appear in a coiled coil.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The residues at the first and fourth side chains of two helices usually form hydrophobic interacting surfaces that are buried in the core. α helix is formed when the peptide bond (C=O) of the nth residue points along the helical axis toward the peptide N-H group of the (n+4)th residue. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Answer 9

(b)

Summary Introduction

To explain: The reason behind the sequence Ile-Gln-Glu-Val-Glu-Arg-Arp is more likely than the sequence Trp-Gln-Glu-Tyr-Glu-Arg-Asp to appear in a coiled coil.

Concept introduction: The secondary structure is the formation of alpha helix and beta-pleated sheets. The residues at the first and fourth side chains of two helices usually form hydrophobic interacting surfaces that are buried in the core. α helix is formed when the peptide bond (C=O) of the nth residue points along the helical axis toward the peptide N-H group of the (n+4)th residue. β sheets are formed, when the hydrogen bonds between the parallel and anti-parallel strands of protein.

Answer 10

Expert Solution & Answer

Answer 11

Expert Solution & Answer

Answer 12

Want to see the full answer?

Check out a sample textbook solution

See solution

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...

Want to see the full answer?

Chapter 6 Solutions