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 protein is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular weight of 200kD. When this protein is run on SDS-PAGE , a sing band is observed at 100kD. Based on these observations, what can be concluded about the structure of the protein? (if applies, choose more than one) The protein consist of two 200kD subiunits The protein has a quaternary structure The protein is madeup of two 100 kD subunits Proteins is a tetramer consisting of 200 kD domains. The protein contains an impurity of 100kD

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 protein is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular weight of 200kD. When this protein is run on SDS-PAGE , a sing band is observed at 100kD. Based on these observations, what can be concluded about the structure of the protein? (if applies, choose more than one) The protein consist of two 200kD subiunits The protein has a quaternary structure The protein is madeup of two 100 kD subunits Proteins is a tetramer consisting of 200 kD domains. The protein contains an impurity of 100kD

. Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is true

A protein was purified to homogeneity. Determination of the mass by gel filtration chromatography yields 60 kd. Chromatography in the presence of the denaturing agent, 6 M urea, yields a 30 kd species. When the chromatography is repeated in the presence of 6 M urea and DTT, a single molecular species of 15 kd results. Describe what these experiments tell you about the structure of the proteins.