The description of the structure of the molecule resulted from the 6M urea and 10 mM ß-mercaptoethanol should be determined. Concept introduction: Gel filtration chromatography is a type of chromatography. It is useful in the separation of proteins based on size. It is also known as the gel permeation or molecular exclusion chromatography.

Question

A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the native protein has a molecular weight of 300,000. Chromatography of the protein in the presence of 6 M guanidine hydrochloride (a denaturant) yields a single peak corresponding to a molecular weight of 50,000. Chromatography of the protein in the presence of 6 M guanidine hydrochloride and 10 mM beta-mercaptoethanol (a disulfide bond reductant) yields peaks corresponding to molecular weights of 30,000 and 20,000. What does this data tell you about the structure of this protein? (Be thorough in your answer!)

Answer 1

Question

Chapter 3, Problem 21P

Interpretation Introduction

Interpretation:

The description of the structure of the molecule resulted from the 6M urea and 10 mM ß-mercaptoethanol should be determined.

Concept introduction:

Gel filtration chromatography is a type of chromatography. It is useful in the separation of proteins based on size. It is also known as the gel permeation or molecular exclusion chromatography.

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A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the native protein has a molecular weight of 300,000. Chromatography of the protein in the presence of 6 M guanidine hydrochloride (a denaturant) yields a single peak corresponding to a molecular weight of 50,000. Chromatography of the protein in the presence of 6 M guanidine hydrochloride and 10 mM beta-mercaptoethanol (a disulfide bond reductant) yields peaks corresponding to molecular weights of 30,000 and 20,000. What does this data tell you about the structure of this protein? (Be thorough in your answer!)

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