An explanation regarding the cleavage of the given amide substrate A by chymotrypsin reveals no burst by using stopped-flow kinetic methods is to be stated. Concept introduction: The organic compounds that contain amine ( -NH 2 ) and carboxyl ( -COOH ) functional groups with a side chain ( -R ) are known as amino acids. Amino acids consist of both positive as well negative groups in their structure and are called as ampholytes. The small chain of amino acids that is connected with the help of the amide bonds is known as peptide. A peptide possesses the covalent bonds which are formed by the reaction of carboxyl group of one amino acid with the amino group of other amino acids. Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction.

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Answer 1

Question

Chapter 9, Problem 1P

Interpretation Introduction

Interpretation: An explanation regarding the cleavage of the given amide substrate A by chymotrypsin reveals no burst by using stopped-flow kinetic methods is to be stated.

Concept introduction: The organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups with a side chain (-R) are known as amino acids. Amino acids consist of both positive as well negative groups in their structure and are called as ampholytes. The small chain of amino acids that is connected with the help of the amide bonds is known as peptide. A peptide possesses the covalent bonds which are formed by the reaction of carboxyl group of one amino acid with the amino group of other amino acids.

Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction.

Expert Solution & Answer

Answer to Problem 1P

The cleavage of the given amide substrate, A, by chymotrypsin reveals no burst because the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate.

Explanation of Solution

Given:

Biochemistry, Chapter 9, Problem 1P

Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction. In case of large hydrophobic amino acids, the cleavage of the peptide bond occurs particularly at the carboxyl-terminal side. In the given amide substrate A, the cleavage by chymotrypsin shows no burst because the hydrolysis for this substrate of amide is faster than the generation of the acyl-enzyme intermediate. In other words, the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate. Hence, no burst is found. In case of ester substrates, the acyl-enzyme intermediate formation occurs at a faster rate.

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In 1956, E. P. Kennedy and S. B. Weiss published their study of membrane lipid phosphatidylcholine (lecithin) synthesis in rat liver. Their hypothesis was that phosphocholine joined with some cellular component to yield lecithin. In an earlier experiment, incubating 32 P-labeled phosphocholine at physiological temperature (37 °C) with broken cells from rat liver yielded labeled lecithin. This became their assay for the enzymes involved in lecithin synthesis. Determine the optimal pH for this enzyme and characterize the enzyme activity at different pH values. -O-P-O-CH2-CH₁₂-N(CH3)3 Phosphocholine H₂C-O-C-R HC-O-C-R2 + + + Cell fraction + ? HC-O-P-O-CH₁₂-CH₂-N(CH), O Phosphatidylcholine The researchers then centrifuged the broken cell preparation to separate the membranes from the soluble proteins. They tested three preparations: whole extract, membranes, and soluble proteins. Table 1 summarizes the results. Table 1: Cell fraction requirement for incorporation of 32p-phosphocholine into…

Researchers isolated an unknown substance, X, from rabbit muscle. They determined its structure from the following observations and experiments. (a) Qualitative analysis showed that X was composed entirely of C, H, and O. A weighed sample of X was completely oxidized and the H2O and CO2 produced were measured. This quantitative analysis revealed that X contained 40.00% C, 6.71% H, and 53.29% O by weight. (b) The molecular mass of X, as determined by mass spectrometry, was 90.00 atomic mass units (u). (c) Infrared spectroscopy showed that X contained one double bond. (d) X dissolved readily in water, and the solution demonstrated optical activity when tested in a polarimeter. (e) The aqueous solution of X is acidic. What is the empirical formula of X?

Show work. don't give Ai generated solution....give correct solution

Answer 2

Question

Chapter 9, Problem 1P

Interpretation Introduction

Interpretation: An explanation regarding the cleavage of the given amide substrate A by chymotrypsin reveals no burst by using stopped-flow kinetic methods is to be stated.

Concept introduction: The organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups with a side chain (-R) are known as amino acids. Amino acids consist of both positive as well negative groups in their structure and are called as ampholytes. The small chain of amino acids that is connected with the help of the amide bonds is known as peptide. A peptide possesses the covalent bonds which are formed by the reaction of carboxyl group of one amino acid with the amino group of other amino acids.

Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction.

Expert Solution & Answer

Answer to Problem 1P

The cleavage of the given amide substrate, A, by chymotrypsin reveals no burst because the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate.

Explanation of Solution

Given:

Biochemistry, Chapter 9, Problem 1P

Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction. In case of large hydrophobic amino acids, the cleavage of the peptide bond occurs particularly at the carboxyl-terminal side. In the given amide substrate A, the cleavage by chymotrypsin shows no burst because the hydrolysis for this substrate of amide is faster than the generation of the acyl-enzyme intermediate. In other words, the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate. Hence, no burst is found. In case of ester substrates, the acyl-enzyme intermediate formation occurs at a faster rate.

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Answer 3

Question

Chapter 9, Problem 1P

Interpretation Introduction

Interpretation: An explanation regarding the cleavage of the given amide substrate A by chymotrypsin reveals no burst by using stopped-flow kinetic methods is to be stated.

Concept introduction: The organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups with a side chain (-R) are known as amino acids. Amino acids consist of both positive as well negative groups in their structure and are called as ampholytes. The small chain of amino acids that is connected with the help of the amide bonds is known as peptide. A peptide possesses the covalent bonds which are formed by the reaction of carboxyl group of one amino acid with the amino group of other amino acids.

Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction.

Expert Solution & Answer

Answer to Problem 1P

The cleavage of the given amide substrate, A, by chymotrypsin reveals no burst because the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate.

Explanation of Solution

Given:

Biochemistry, Chapter 9, Problem 1P

Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction. In case of large hydrophobic amino acids, the cleavage of the peptide bond occurs particularly at the carboxyl-terminal side. In the given amide substrate A, the cleavage by chymotrypsin shows no burst because the hydrolysis for this substrate of amide is faster than the generation of the acyl-enzyme intermediate. In other words, the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate. Hence, no burst is found. In case of ester substrates, the acyl-enzyme intermediate formation occurs at a faster rate.

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Answer 4

Question

Chapter 9, Problem 1P

Interpretation Introduction

Interpretation: An explanation regarding the cleavage of the given amide substrate A by chymotrypsin reveals no burst by using stopped-flow kinetic methods is to be stated.

Concept introduction: The organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups with a side chain (-R) are known as amino acids. Amino acids consist of both positive as well negative groups in their structure and are called as ampholytes. The small chain of amino acids that is connected with the help of the amide bonds is known as peptide. A peptide possesses the covalent bonds which are formed by the reaction of carboxyl group of one amino acid with the amino group of other amino acids.

Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction.

Expert Solution & Answer

Answer to Problem 1P

The cleavage of the given amide substrate, A, by chymotrypsin reveals no burst because the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate.

Explanation of Solution

Given:

Biochemistry, Chapter 9, Problem 1P

Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction. In case of large hydrophobic amino acids, the cleavage of the peptide bond occurs particularly at the carboxyl-terminal side. In the given amide substrate A, the cleavage by chymotrypsin shows no burst because the hydrolysis for this substrate of amide is faster than the generation of the acyl-enzyme intermediate. In other words, the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate. Hence, no burst is found. In case of ester substrates, the acyl-enzyme intermediate formation occurs at a faster rate.

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Answer 5

Chapter 9, Problem 1P

Interpretation Introduction

Interpretation: An explanation regarding the cleavage of the given amide substrate A by chymotrypsin reveals no burst by using stopped-flow kinetic methods is to be stated.

Concept introduction: The organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups with a side chain (-R) are known as amino acids. Amino acids consist of both positive as well negative groups in their structure and are called as ampholytes. The small chain of amino acids that is connected with the help of the amide bonds is known as peptide. A peptide possesses the covalent bonds which are formed by the reaction of carboxyl group of one amino acid with the amino group of other amino acids.

Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction.

Expert Solution & Answer

Answer to Problem 1P

The cleavage of the given amide substrate, A, by chymotrypsin reveals no burst because the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate.

Explanation of Solution

Given:

Biochemistry, Chapter 9, Problem 1P

Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction. In case of large hydrophobic amino acids, the cleavage of the peptide bond occurs particularly at the carboxyl-terminal side. In the given amide substrate A, the cleavage by chymotrypsin shows no burst because the hydrolysis for this substrate of amide is faster than the generation of the acyl-enzyme intermediate. In other words, the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate. Hence, no burst is found. In case of ester substrates, the acyl-enzyme intermediate formation occurs at a faster rate.

Answer 6

Chapter 9, Problem 1P

Interpretation Introduction

Interpretation: An explanation regarding the cleavage of the given amide substrate A by chymotrypsin reveals no burst by using stopped-flow kinetic methods is to be stated.

Concept introduction: The organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups with a side chain (-R) are known as amino acids. Amino acids consist of both positive as well negative groups in their structure and are called as ampholytes. The small chain of amino acids that is connected with the help of the amide bonds is known as peptide. A peptide possesses the covalent bonds which are formed by the reaction of carboxyl group of one amino acid with the amino group of other amino acids.

Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction.

Expert Solution & Answer

Answer to Problem 1P

The cleavage of the given amide substrate, A, by chymotrypsin reveals no burst because the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate.

Explanation of Solution

Given:

Biochemistry, Chapter 9, Problem 1P

Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction. In case of large hydrophobic amino acids, the cleavage of the peptide bond occurs particularly at the carboxyl-terminal side. In the given amide substrate A, the cleavage by chymotrypsin shows no burst because the hydrolysis for this substrate of amide is faster than the generation of the acyl-enzyme intermediate. In other words, the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate. Hence, no burst is found. In case of ester substrates, the acyl-enzyme intermediate formation occurs at a faster rate.

Answer 7

Chapter 9, Problem 1P

Interpretation Introduction

Interpretation: An explanation regarding the cleavage of the given amide substrate A by chymotrypsin reveals no burst by using stopped-flow kinetic methods is to be stated.

Concept introduction: The organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups with a side chain (-R) are known as amino acids. Amino acids consist of both positive as well negative groups in their structure and are called as ampholytes. The small chain of amino acids that is connected with the help of the amide bonds is known as peptide. A peptide possesses the covalent bonds which are formed by the reaction of carboxyl group of one amino acid with the amino group of other amino acids.

Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction.

Answer 8

Expert Solution & Answer

Answer to Problem 1P

The cleavage of the given amide substrate, A, by chymotrypsin reveals no burst because the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate.

Answer 9

Expert Solution & Answer

Answer 10

Expert Solution & Answer

Answer 11

Explanation of Solution

Given:

Biochemistry, Chapter 9, Problem 1P

Chymotrypsin is an enzyme that is used for the cleavage of protein through hydrolysis reaction. In case of large hydrophobic amino acids, the cleavage of the peptide bond occurs particularly at the carboxyl-terminal side. In the given amide substrate A, the cleavage by chymotrypsin shows no burst because the hydrolysis for this substrate of amide is faster than the generation of the acyl-enzyme intermediate. In other words, the acyl-enzyme intermediate formation occurs at a slower rate as compared to the hydrolysis for the given amide substrate. Hence, no burst is found. In case of ester substrates, the acyl-enzyme intermediate formation occurs at a faster rate.

Answer 12

Ch. 9 - Prob. 1P Ch. 9 - Prob. 2P Ch. 9 - Prob. 3P Ch. 9 - Prob. 4P Ch. 9 - Prob. 5P Ch. 9 - Prob. 6P Ch. 9 - Prob. 7P Ch. 9 - Prob. 8P Ch. 9 - Prob. 9P Ch. 9 - Prob. 10P

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