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!)

The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).

Purification of a protein of unknown structure has been achieved. The natural protein has a molecular weight of 240,000, according to size-exclusion chromatography. Using a concentration of 6 M guanidine hydrochloride in the chromatography, a single peak can be identified as the molecular weight (MW) 60,000 of a protein. B-mercaptoethanol (BME) and guanidine hydrochloride (GHC) are used in tandem to produce proteins with mass masses of 34,000 and 26,000, respectively. The structure of this protein can be inferred from these facts.