The tetrapeptide which will produce the same fragments when treated with chymotrypsin need to be identified. 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 enzyme 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 tetrapeptide which gives the same two fragments when treated with chymotrypsin.

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Answer 1

Question

Chapter 25.5, Problem 32ATS

Interpretation Introduction

Interpretation:

The tetrapeptide which will produce the same fragments when treated with chymotrypsin need to be identified.

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 enzyme 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 tetrapeptide which gives the same two fragments when treated with chymotrypsin.

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Answer 2

Question

Chapter 25.5, Problem 32ATS

Interpretation Introduction

Interpretation:

The tetrapeptide which will produce the same fragments when treated with chymotrypsin need to be identified.

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 enzyme 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 tetrapeptide which gives the same two fragments when treated with chymotrypsin.

Expert Solution & Answer

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Check out a sample textbook solution

See solution

Answer 3

Question

Chapter 25.5, Problem 32ATS

Interpretation Introduction

Interpretation:

The tetrapeptide which will produce the same fragments when treated with chymotrypsin need to be identified.

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 enzyme 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 tetrapeptide which gives the same two fragments when treated with chymotrypsin.

Expert Solution & Answer

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Check out a sample textbook solution

See solution

Answer 4

Question

Chapter 25.5, Problem 32ATS

Interpretation Introduction

Interpretation:

The tetrapeptide which will produce the same fragments when treated with chymotrypsin need to be identified.

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 enzyme 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 tetrapeptide which gives the same two fragments when treated with chymotrypsin.

Expert Solution & Answer

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Check out a sample textbook solution

See solution

Answer 5

Chapter 25.5, Problem 32ATS

Interpretation Introduction

Interpretation:

The tetrapeptide which will produce the same fragments when treated with chymotrypsin need to be identified.

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 enzyme 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 tetrapeptide which gives the same two fragments when treated with chymotrypsin.

Answer 6

Chapter 25.5, Problem 32ATS

Interpretation Introduction

Interpretation:

The tetrapeptide which will produce the same fragments when treated with chymotrypsin need to be identified.

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 enzyme 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 tetrapeptide which gives the same two fragments when treated with chymotrypsin.

Answer 7

Chapter 25.5, Problem 32ATS

Interpretation Introduction

Interpretation:

The tetrapeptide which will produce the same fragments when treated with chymotrypsin need to be identified.

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 enzyme 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 tetrapeptide which gives the same two fragments when treated with chymotrypsin.

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