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Chapter 6: Problem 7

A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the native protein has a molecular weight of 240,000 , Chromatography in the presence of \(6 M\) guanidine hydrochloride yields only a peak for a protein of \(M\) \(60,000 .\) Chromatography in the presence of \(6 \mathrm{M}\) guanidine hydrochloride and \(10 \mathrm{m}\) M \(\beta\) -mercaptoethanol yields peaks for proteins of \(M, 34,000\) and \(26,000 .\) Explain what can be determined about the structure of this protein from these data.

Short Answer

Expert verified
The protein in its native form is a tetramer, composed of four 60,000 molecular weight subunits. Each of these subunits is made up of two polypeptide chains, one of molecular weight 34,000 and the other of weight 26,000, held together by disulfide bonds.

Step by step solution

01

Analyze the Protein Structure in its Native State

From gel filtration chromatography, it is known that the native state of the protein has a molecular weight of 240,000. This refers to the protein in its intact, natural form.
02

Analyze the Protein Structure in the presence of 6M Guanidine Hydrochloride

Chromatography in the presence of \(6 M\) guanidine hydrochloride, a denaturant, results in a peak for a protein of \(M\) \(60,000\) . This suggests that guanidine hydrochloride breaks apart the protein into smaller units, each with a molecular weight of 60,000. Hence, it can be inferred that the native 240,000 weight protein is tetrameric, made up of four subunits of 60,000 each.
03

Analyze the Protein Structure in the presence of 6M Guanidine Hydrochloride and 10 mM Beta-mercaptoethanol

Chromatography in the presence of both \(6 M\) guanidine hydrochloride and \(10 mM\) \(\beta\)-mercaptoethanol causes further breakdown. Now, peaks for proteins of \(M, 34,000\) and 26,000 appear. Beta-mercaptoethanol breaks disulfide bonds. The fact that the 60,000 protein breaks down into proteins of 34,000 and 26,000 implies that the 60,000 protein is comprised of two polypeptide chains held together by disulfide bonds.

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Most popular questions from this chapter

Poly-L-glutamate adopts an a-helical structure at low pH but becomes a random coil above pH \(5 .\) Explain this behavior.

Which amino acids would be capable of forming H bonds with a lysine residue in a protein?

Discuss the potential contributions to hydrophobic and van der Waals interactions and ionic and hydrogen bonds for the side chains of Asp, Leu, Tyr, and His in a protein.

Pro is the amino acid least commonly found in \(\alpha\) -helices but most commonly found in \(\beta\) -turns, Discuss the reasons for this behavior.

Choose any three regions in the Ramachandran plot and discuss the likelihood of observing that combination of \(\phi\) and \(\psi\) in a peptide or protein. Defend your answer using suitable molecular models of a peptide.
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