(a) To propose: The strong inhibitory property of the peptide pepstatin Introduction: Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

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Answer 1

Question

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

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Fura-2 Fluorescence (Arbitrary Unit) 4500 4000 3500 3000 2500 2000 1500 1000 500 [Ca2+]=2970nM, 25°C [Ca2+] 2970nM, 4°C [Ca2+]=0.9nM, 25°C [Ca2+] = 0.9nM, 4°C 0 260 280 300 340 360 380 400 420 440 Wavelength (nm) ← < The figure on the LHS shows the excitation spectra of Fura-2 (Em = 510 nm) in 2 solutions with two different Ca2+ ion concentration as indicated. Except for temperature, the setting for excitation & signal acquisition was identical.< ப a) The unit in Y-axis is arbitrary (unspecified). Why? < < b) Compare & contrast the excitation wavelength of the Isosbestic Point of Fura-2 at 25 °C & 4 °C. Give a possible reason for the discrepancy. < c) The fluorescence intensity at 25 °C & 4 °C are different. Explain why with the concept of electronic configuration. <

Answer 2

Question

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

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Answer 3

Question

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Expert Solution & Answer

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Check out a sample textbook solution

See solution

Answer 4

Question

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Expert Solution & Answer

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Answer 5

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 6

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 7

Chapter 14, Problem 3P

Interpretation Introduction

(a)

To propose:

The strong inhibitory property of the peptide pepstatin

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 8

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 9

Interpretation Introduction

(b)

To explain:

Whether the pepstatin exhibit inhibits the HIV-1 protease or not.

Introduction:

Aspartic proteases include the protease enzymes which uses two very active aspartic acid complexes for the cleavage reaction of the peptide substrates. Pepstatin is a naturally present in the cell which has hexa-peptide structure with amino acid Statine and thus generally inhibits aspartyl proteases.

Answer 10

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Answer 11

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Answer 12

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Answer 13

Ch. 14 - Answers to all problems are at the end Î¿Î“this...Ch. 14 - Answers to all problems are at the end Î¿Î“this...Ch. 14 - Prob. 3P Ch. 14 - Prob. 4P Ch. 14 - Answers to all problems are at the end Î¿Î“this...Ch. 14 - Prob. 6P Ch. 14 - Prob. 7P Ch. 14 - Answers to all problems are at the end Î¿Î“this...Ch. 14 - Answers to all problems are at the end Î¿f this...Ch. 14 - Answers to all problems are at the end Î¿f this...

Solution Summary: The author explains that the strong inhibitory property of pepstatin is due to the transformation of the central amino acid to a transition state.

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