The reagents used in the determination of the amino acid sequence of a small peptide should be determined. Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

Question

Want to see more full solutions like this?

Answer 1

Question

Chapter 3, Problem 1P

(a)

Interpretation Introduction

Interpretation: The reagents used in the determination of the amino acid sequence of a small peptide should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(a)

Expert Solution

Answer to Problem 1P

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Explanation of Solution

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Phenyl isothiocyanate shows a reaction with an uncharged N-terminal amino group. It occurs under the slightly alkaline conditions and forms a cyclical phenyl thiocarbamoyl derivative. It can sequence up to 30 amino acids accurately with modern machines. It is proficient of over 99% proficiency per amino acid.

(b)

Interpretation Introduction

Interpretation: The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds should be determined. Also, the reagent needed when the disulfide bonds are present should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(b)

Expert Solution

Answer to Problem 1P

The reagent for the reversible denaturation is urea. Beta-mercaptoethanol is used to reduce the disulfide bonds.

Explanation of Solution

The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds is urea.

If the disulfide bonds are present, then the reagent needed is beta-mercaptoethanol. This reagent is used to reduce the disulfide bonds.

(c)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(c)

Expert Solution

Answer to Problem 1P

The reagent required is chymotrypsin.

Explanation of Solution

The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues is chymotrypsin which specifically cleaves the C-terminal side of aromatic acid residues.

(d)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(d)

Expert Solution

Answer to Problem 1P

The reagent useful for thepeptide bonds cleavage on the carboxyl side of methionine is CNBr or cyanogen bromide.

Explanation of Solution

The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine is CNBr. It is also known as cyanogen bromide. It is a solid and colorless inorganic compound. It is extensively used to change the biopolymers, fragment proteins and peptides. It generally cleaves the C-terminus of methionine and produces other compounds.

(e)

Interpretation Introduction

Interpretation: The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(e)

Expert Solution

Answer to Problem 1P

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Explanation of Solution

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Trypsin is generally formed in the small intestine. It is formed by the activation of trypsinogen. Trypsin usually cuts the peptide chains primarily at the carboxyl side of the lysine or arginineamino acids. It is used for many biotechnological processes.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

Students have asked these similar questions

Biochemistry What is the process of "transamination" in either the muscles or the liver, that involves keto acid or glutamic acid? Please explain how the steps work. Thank you!

Biochemistry Please help. Thank you What is the importance of glutamic acid in the metabolism of nitrogen from amino acids? (we know therole; it’s used to remove the nitrogen from amino acids so that the remaining carbon skeleton can bebroken down by the “usual” pathways, but what is the important, unique role that only glutamicacid/glutamate can do?)

Biochemistry Please help. Thank you When carbamyl phosphate is joined to L-ornathine, where does the energy for the reaction come from?

Answer 2

Question

Chapter 3, Problem 1P

(a)

Interpretation Introduction

Interpretation: The reagents used in the determination of the amino acid sequence of a small peptide should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(a)

Expert Solution

Answer to Problem 1P

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Explanation of Solution

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Phenyl isothiocyanate shows a reaction with an uncharged N-terminal amino group. It occurs under the slightly alkaline conditions and forms a cyclical phenyl thiocarbamoyl derivative. It can sequence up to 30 amino acids accurately with modern machines. It is proficient of over 99% proficiency per amino acid.

(b)

Interpretation Introduction

Interpretation: The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds should be determined. Also, the reagent needed when the disulfide bonds are present should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(b)

Expert Solution

Answer to Problem 1P

The reagent for the reversible denaturation is urea. Beta-mercaptoethanol is used to reduce the disulfide bonds.

Explanation of Solution

The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds is urea.

If the disulfide bonds are present, then the reagent needed is beta-mercaptoethanol. This reagent is used to reduce the disulfide bonds.

(c)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(c)

Expert Solution

Answer to Problem 1P

The reagent required is chymotrypsin.

Explanation of Solution

The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues is chymotrypsin which specifically cleaves the C-terminal side of aromatic acid residues.

(d)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(d)

Expert Solution

Answer to Problem 1P

The reagent useful for thepeptide bonds cleavage on the carboxyl side of methionine is CNBr or cyanogen bromide.

Explanation of Solution

The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine is CNBr. It is also known as cyanogen bromide. It is a solid and colorless inorganic compound. It is extensively used to change the biopolymers, fragment proteins and peptides. It generally cleaves the C-terminus of methionine and produces other compounds.

(e)

Interpretation Introduction

Interpretation: The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(e)

Expert Solution

Answer to Problem 1P

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Explanation of Solution

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Trypsin is generally formed in the small intestine. It is formed by the activation of trypsinogen. Trypsin usually cuts the peptide chains primarily at the carboxyl side of the lysine or arginineamino acids. It is used for many biotechnological processes.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

Answer 3

Question

Chapter 3, Problem 1P

(a)

Interpretation Introduction

Interpretation: The reagents used in the determination of the amino acid sequence of a small peptide should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(a)

Expert Solution

Answer to Problem 1P

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Explanation of Solution

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Phenyl isothiocyanate shows a reaction with an uncharged N-terminal amino group. It occurs under the slightly alkaline conditions and forms a cyclical phenyl thiocarbamoyl derivative. It can sequence up to 30 amino acids accurately with modern machines. It is proficient of over 99% proficiency per amino acid.

(b)

Interpretation Introduction

Interpretation: The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds should be determined. Also, the reagent needed when the disulfide bonds are present should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(b)

Expert Solution

Answer to Problem 1P

The reagent for the reversible denaturation is urea. Beta-mercaptoethanol is used to reduce the disulfide bonds.

Explanation of Solution

The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds is urea.

If the disulfide bonds are present, then the reagent needed is beta-mercaptoethanol. This reagent is used to reduce the disulfide bonds.

(c)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(c)

Expert Solution

Answer to Problem 1P

The reagent required is chymotrypsin.

Explanation of Solution

The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues is chymotrypsin which specifically cleaves the C-terminal side of aromatic acid residues.

(d)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(d)

Expert Solution

Answer to Problem 1P

The reagent useful for thepeptide bonds cleavage on the carboxyl side of methionine is CNBr or cyanogen bromide.

Explanation of Solution

The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine is CNBr. It is also known as cyanogen bromide. It is a solid and colorless inorganic compound. It is extensively used to change the biopolymers, fragment proteins and peptides. It generally cleaves the C-terminus of methionine and produces other compounds.

(e)

Interpretation Introduction

Interpretation: The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(e)

Expert Solution

Answer to Problem 1P

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Explanation of Solution

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Trypsin is generally formed in the small intestine. It is formed by the activation of trypsinogen. Trypsin usually cuts the peptide chains primarily at the carboxyl side of the lysine or arginineamino acids. It is used for many biotechnological processes.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

Answer 4

Question

Chapter 3, Problem 1P

(a)

Interpretation Introduction

Interpretation: The reagents used in the determination of the amino acid sequence of a small peptide should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(a)

Expert Solution

Answer to Problem 1P

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Explanation of Solution

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Phenyl isothiocyanate shows a reaction with an uncharged N-terminal amino group. It occurs under the slightly alkaline conditions and forms a cyclical phenyl thiocarbamoyl derivative. It can sequence up to 30 amino acids accurately with modern machines. It is proficient of over 99% proficiency per amino acid.

(b)

Interpretation Introduction

Interpretation: The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds should be determined. Also, the reagent needed when the disulfide bonds are present should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(b)

Expert Solution

Answer to Problem 1P

The reagent for the reversible denaturation is urea. Beta-mercaptoethanol is used to reduce the disulfide bonds.

Explanation of Solution

The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds is urea.

If the disulfide bonds are present, then the reagent needed is beta-mercaptoethanol. This reagent is used to reduce the disulfide bonds.

(c)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(c)

Expert Solution

Answer to Problem 1P

The reagent required is chymotrypsin.

Explanation of Solution

The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues is chymotrypsin which specifically cleaves the C-terminal side of aromatic acid residues.

(d)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(d)

Expert Solution

Answer to Problem 1P

The reagent useful for thepeptide bonds cleavage on the carboxyl side of methionine is CNBr or cyanogen bromide.

Explanation of Solution

The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine is CNBr. It is also known as cyanogen bromide. It is a solid and colorless inorganic compound. It is extensively used to change the biopolymers, fragment proteins and peptides. It generally cleaves the C-terminus of methionine and produces other compounds.

(e)

Interpretation Introduction

Interpretation: The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(e)

Expert Solution

Answer to Problem 1P

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Explanation of Solution

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Trypsin is generally formed in the small intestine. It is formed by the activation of trypsinogen. Trypsin usually cuts the peptide chains primarily at the carboxyl side of the lysine or arginineamino acids. It is used for many biotechnological processes.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!

Answer 5

Chapter 3, Problem 1P

(a)

Interpretation Introduction

Interpretation: The reagents used in the determination of the amino acid sequence of a small peptide should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(a)

Expert Solution

Answer to Problem 1P

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Explanation of Solution

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Phenyl isothiocyanate shows a reaction with an uncharged N-terminal amino group. It occurs under the slightly alkaline conditions and forms a cyclical phenyl thiocarbamoyl derivative. It can sequence up to 30 amino acids accurately with modern machines. It is proficient of over 99% proficiency per amino acid.

(b)

Interpretation Introduction

Interpretation: The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds should be determined. Also, the reagent needed when the disulfide bonds are present should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(b)

Expert Solution

Answer to Problem 1P

The reagent for the reversible denaturation is urea. Beta-mercaptoethanol is used to reduce the disulfide bonds.

Explanation of Solution

The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds is urea.

If the disulfide bonds are present, then the reagent needed is beta-mercaptoethanol. This reagent is used to reduce the disulfide bonds.

(c)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(c)

Expert Solution

Answer to Problem 1P

The reagent required is chymotrypsin.

Explanation of Solution

The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues is chymotrypsin which specifically cleaves the C-terminal side of aromatic acid residues.

(d)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(d)

Expert Solution

Answer to Problem 1P

The reagent useful for thepeptide bonds cleavage on the carboxyl side of methionine is CNBr or cyanogen bromide.

Explanation of Solution

The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine is CNBr. It is also known as cyanogen bromide. It is a solid and colorless inorganic compound. It is extensively used to change the biopolymers, fragment proteins and peptides. It generally cleaves the C-terminus of methionine and produces other compounds.

(e)

Interpretation Introduction

Interpretation: The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(e)

Expert Solution

Answer to Problem 1P

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Explanation of Solution

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Trypsin is generally formed in the small intestine. It is formed by the activation of trypsinogen. Trypsin usually cuts the peptide chains primarily at the carboxyl side of the lysine or arginineamino acids. It is used for many biotechnological processes.

Answer 6

Chapter 3, Problem 1P

(a)

Interpretation Introduction

Interpretation: The reagents used in the determination of the amino acid sequence of a small peptide should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(a)

Expert Solution

Answer to Problem 1P

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Explanation of Solution

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Phenyl isothiocyanate shows a reaction with an uncharged N-terminal amino group. It occurs under the slightly alkaline conditions and forms a cyclical phenyl thiocarbamoyl derivative. It can sequence up to 30 amino acids accurately with modern machines. It is proficient of over 99% proficiency per amino acid.

Answer 7

Chapter 3, Problem 1P

(a)

Interpretation Introduction

Interpretation: The reagents used in the determination of the amino acid sequence of a small peptide should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

Answer 8

(a)

Expert Solution

Answer to Problem 1P

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Answer 9

(a)

Expert Solution

Answer 10

(a)

Expert Solution

Answer 11

Expert Solution

Answer 12

Explanation of Solution

The reagent used in the determination of the amino acid sequence of a small peptide is phenyl isothiocyanate.

Phenyl isothiocyanate shows a reaction with an uncharged N-terminal amino group. It occurs under the slightly alkaline conditions and forms a cyclical phenyl thiocarbamoyl derivative. It can sequence up to 30 amino acids accurately with modern machines. It is proficient of over 99% proficiency per amino acid.

Answer 13

(b)

Interpretation Introduction

Interpretation: The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds should be determined. Also, the reagent needed when the disulfide bonds are present should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(b)

Expert Solution

Answer to Problem 1P

The reagent for the reversible denaturation is urea. Beta-mercaptoethanol is used to reduce the disulfide bonds.

Explanation of Solution

The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds is urea.

If the disulfide bonds are present, then the reagent needed is beta-mercaptoethanol. This reagent is used to reduce the disulfide bonds.

Answer 14

(b)

Interpretation Introduction

Interpretation: The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds should be determined. Also, the reagent needed when the disulfide bonds are present should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

Answer 15

(b)

Expert Solution

Answer to Problem 1P

The reagent for the reversible denaturation is urea. Beta-mercaptoethanol is used to reduce the disulfide bonds.

Answer 16

(b)

Expert Solution

Answer 17

(b)

Expert Solution

Answer 18

Expert Solution

Answer 19

Explanation of Solution

The reagent that can undergo reversible denaturation if a protein lacks disulfide bonds is urea.

If the disulfide bonds are present, then the reagent needed is beta-mercaptoethanol. This reagent is used to reduce the disulfide bonds.

Answer 20

(c)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(c)

Expert Solution

Answer to Problem 1P

The reagent required is chymotrypsin.

Explanation of Solution

The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues is chymotrypsin which specifically cleaves the C-terminal side of aromatic acid residues.

Answer 21

(c)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

Answer 22

(c)

Expert Solution

Answer to Problem 1P

The reagent required is chymotrypsin.

Answer 23

(c)

Expert Solution

Answer 24

(c)

Expert Solution

Answer 25

Expert Solution

Answer 26

Explanation of Solution

The reagent useful for the peptide bonds hydrolysis present on the carboxyl side of aromatic residues is chymotrypsin which specifically cleaves the C-terminal side of aromatic acid residues.

Answer 27

(d)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(d)

Expert Solution

Answer to Problem 1P

The reagent useful for thepeptide bonds cleavage on the carboxyl side of methionine is CNBr or cyanogen bromide.

Explanation of Solution

The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine is CNBr. It is also known as cyanogen bromide. It is a solid and colorless inorganic compound. It is extensively used to change the biopolymers, fragment proteins and peptides. It generally cleaves the C-terminus of methionine and produces other compounds.

Answer 28

(d)

Interpretation Introduction

Interpretation: The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

Answer 29

(d)

Expert Solution

Answer to Problem 1P

The reagent useful for thepeptide bonds cleavage on the carboxyl side of methionine is CNBr or cyanogen bromide.

Answer 30

(d)

Expert Solution

Answer 31

(d)

Expert Solution

Answer 32

Expert Solution

Answer 33

Explanation of Solution

The reagent useful for the peptide bonds cleavage on the carboxyl side of methionine is CNBr. It is also known as cyanogen bromide. It is a solid and colorless inorganic compound. It is extensively used to change the biopolymers, fragment proteins and peptides. It generally cleaves the C-terminus of methionine and produces other compounds.

Answer 34

(e)

Interpretation Introduction

Interpretation: The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

(e)

Expert Solution

Answer to Problem 1P

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Explanation of Solution

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Trypsin is generally formed in the small intestine. It is formed by the activation of trypsinogen. Trypsin usually cuts the peptide chains primarily at the carboxyl side of the lysine or arginineamino acids. It is used for many biotechnological processes.

Answer 35

(e)

Interpretation Introduction

Interpretation: The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues should be determined.

Concept Introduction: A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.

Answer 36

(e)

Expert Solution

Answer to Problem 1P

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Answer 37

(e)

Expert Solution

Answer 38

(e)

Expert Solution

Answer 39

Expert Solution

Answer 40

Explanation of Solution

The reagent for hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues is trypsin.

Trypsin is generally formed in the small intestine. It is formed by the activation of trypsinogen. Trypsin usually cuts the peptide chains primarily at the carboxyl side of the lysine or arginineamino acids. It is used for many biotechnological processes.