The sequence of 16 amino acid residues in starting peptide need to be identified from the given trypsin and chymotrypsin fragments. Concept introduction: Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzymes are trypsin and chymotrypsin. Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine. Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan. To identify : the sequence of 16 amino acid residue in the starting peptide.

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Answer 1

Question

Chapter 25.5, Problem 4LTS

Interpretation Introduction

Interpretation:

The sequence of 16 amino acid residues in starting peptide need to be identified from the given trypsin and chymotrypsin fragments.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzymes are trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To identify: the sequence of 16 amino acid residue in the starting peptide.

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Answer 2

Question

Chapter 25.5, Problem 4LTS

Interpretation Introduction

Interpretation:

The sequence of 16 amino acid residues in starting peptide need to be identified from the given trypsin and chymotrypsin fragments.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzymes are trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To identify: the sequence of 16 amino acid residue in the starting peptide.

Expert Solution & Answer

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Answer 3

Question

Chapter 25.5, Problem 4LTS

Interpretation Introduction

Interpretation:

The sequence of 16 amino acid residues in starting peptide need to be identified from the given trypsin and chymotrypsin fragments.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzymes are trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To identify: the sequence of 16 amino acid residue in the starting peptide.

Expert Solution & Answer

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Answer 4

Question

Chapter 25.5, Problem 4LTS

Interpretation Introduction

Interpretation:

The sequence of 16 amino acid residues in starting peptide need to be identified from the given trypsin and chymotrypsin fragments.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzymes are trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To identify: the sequence of 16 amino acid residue in the starting peptide.

Expert Solution & Answer

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Answer 5

Chapter 25.5, Problem 4LTS

Interpretation Introduction

Interpretation:

The sequence of 16 amino acid residues in starting peptide need to be identified from the given trypsin and chymotrypsin fragments.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzymes are trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To identify: the sequence of 16 amino acid residue in the starting peptide.

Answer 6

Chapter 25.5, Problem 4LTS

Interpretation Introduction

Interpretation:

The sequence of 16 amino acid residues in starting peptide need to be identified from the given trypsin and chymotrypsin fragments.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzymes are trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To identify: the sequence of 16 amino acid residue in the starting peptide.

Answer 7

Chapter 25.5, Problem 4LTS

Interpretation Introduction

Interpretation:

The sequence of 16 amino acid residues in starting peptide need to be identified from the given trypsin and chymotrypsin fragments.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzymes are trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

To identify: the sequence of 16 amino acid residue in the starting peptide.

Answer 8

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Answer 9

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Answer 10

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Answer 11

Ch. 25.2 - Prob. 1CC Ch. 25.2 - Prob. 2CC Ch. 25.2 - Prob. 3CC Ch. 25.2 - Prob. 1LTS Ch. 25.2 - Prob. 4PTS Ch. 25.2 - Prob. 5ATS Ch. 25.2 - Prob. 6ATS Ch. 25.2 - Prob. 7CC Ch. 25.2 - Prob. 8CC Ch. 25.2 - Prob. 9CC

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Chapter 25 Solutions