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Use the given experimental data to deduce the sequence of an octapeptide that contains the following amino acids: Ala, Gly (2 equiv), His (2 equiv), Ile, Leu and Phe. Edman degradation cleaves Gly from the octapeptide, and carboxypeptidase forms Leu and a heptapeptide. Partial hydrolysis forms the following fragments: Ile-His-Leu, Gly, Gly-Ala-Phe-His, and Phe-His-Ile.

Short Answer

Expert verified

The sequence of an octapeptide is Gly-Gly-Ala-Phe-His-Ile-His-Leu.

Step by step solution

01

Octapeptide

An octapeptide is a continuous polypeptide chain and contains eight amino acids.It cleaves into smaller fragments when octapeptide is treated with chymotrypsin, trypsin, and carboxypeptidase.

02

Sequence of an octapeptide.

The given fragments are Ile-His-Leu, Gly, Gly-Ala-Phe-His, and Phe-His-Ile.

Here, Phe-His-Ile has Phe-His common to Gly-Ala-Phe-His and Ile is common to Ile-His-Leu. These three fragments are joined together by taking common amino acids as one.

The sequence of octapeptide obtained is Gly-Gly-Ala-Phe-His-Ile-His-Leu. Gly comes at the front of the sequence as it is cleaved by Edman degradation, and Leu comes at last because carboxypeptidase forms Leu and heptapeptide.

The sequence of an octapeptide

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Most popular questions from this chapter

What steps are needed to convert A to L-dopa, an uncommon amino acid that is effective in treating Parkinsonโ€™s disease? These steps are the key reactions in the first commercial asymmetric synthesis using a chiral transition metal catalyst. This process was developed at Monsanto in 1974.

a. Draw the structure of the tripeptide A-A-A, and label the two ionizable functional groups.

b. What is the predominant form of A-A-A at pH=1?

c. ThepKa values for the two ionizable functional groups (3.39 and 8.03) differ considerably from thepKa values of alanine (2.35 and 9.87;see table 29.1). Account for the observedpKa differences.

Deduce the sequence of a heptapeptide that contains the amino acids Ala, Arg, Glu, Gly, Leu, Phe, and Ser, from the following experimental data. Edman degradation cleaves Leu from the heptapeptide, and carboxypeptidase forms Glu and a hexapeptide. Treatment of the heptapeptide with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Glu, Leu, Phe, and the tripeptidesGlyโ€“Alaโ€“Ser and Alaโ€“Serโ€“Arg

Draw the organic products formed in each reaction.

Another strategy used to resolve amino acids involves converting the carboxy group to an ester and then using a chiral carboxylic acid to carry out an acid-base reaction at the free amino group. Using a racemic mixture of alanine enantiomers and (R)-mandelic acid as resolving agent, write out the steps showing how a resolution process would occur.

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