The sequence of the peptide consisting of 14 amino acids should be determined. Concept introduction: Trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine (K) or arginine (R) if they are not followed by proline. Carboxypeptidase hydrolyzes the first peptide bond at the C-terminal of the peptide chain except for arginine (R), lysine (K) or proline (P). Chymotrypsin cleaves the peptide bond at the C-terminal where there ishydrophobic amino acids like tyrosine (Y), tryptophan (W), phenylalanine (F), leucine (L) and methionine (M). Cyanogen bromide hydrolyzes peptide bond at C-terminal of methionine residues. Homoserine is a product of cyanogen bromide cleavage by degradation of methionine.

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 27P

Interpretation Introduction

Interpretation:

The sequence of the peptide consisting of 14 amino acids should be determined.

Concept introduction:

Trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine (K) or arginine (R) if they are not followed by proline. Carboxypeptidase hydrolyzes the first peptide bond at the C-terminal of the peptide chain except for arginine (R), lysine (K) or proline (P). Chymotrypsin cleaves the peptide bond at the C-terminal where there ishydrophobic amino acids like tyrosine (Y), tryptophan (W), phenylalanine (F), leucine (L) and methionine (M). Cyanogen bromide hydrolyzes peptide bond at C-terminal of methionine residues. Homoserine is a product of cyanogen bromide cleavage by degradation of methionine.

Expert Solution & Answer

Trending nowThis is a popular solution!

See solution

Check out sample textbook solution

Students have asked these similar questions

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!)

pls answer the following question. -Which amino acids contain the following?a.sulfur/sulfhydryl group b. aromatic group c. imidazole ring d. guanidine group e. indole group -Classify the following proteins according to their biological function: casein, albumin gluten, and myoglobin. -Which levels of protein structure organization are lost during hydrolysis and denaturation? -What is the Beer-Lambert's Law? Why is it relevant to the quantitative analysis of proteins? -What are the other protein components of milk aside from casein?

(a) How is ubiquitination attached to the protein of interest? At which amino acid residue(s)? What enzyme(s) is involved, if any?(b) Is the ubiquitination relatively stable or highly dynamic? how does ubiquitination become detached from the protein of interest? what enzyme is involved?(c) what is the function of ubiquitination