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Chapter 24: Q22P (page 1283)

Show where trypsin and chymotrypsin would cleave the following peptide.

Tyr-Ile-Gln-Arg-Leu-Gly-Phe-Lys-Asn-Trp-Phe-Gly-Ala-Lys-Gly-Gln-Gln.NH2

Short Answer

Expert verified

Trypsin is an enzyme and it breaks down protein into amino acids. It cleaves at the carboxyl side or C-terminal side of the amino acids lysine and arginine.

Cleavage sites of Trypsin

Step by step solution

01

Step-1. Action of trypsin on peptide chain:

Trypsin is an enzyme and it breaks down protein into amino acids. It cleaves at the carboxyl side or C-terminal side of the amino acids lysine and arginine.

Cleavage sites of Trypsin

02

Step-2. Action of chymotrypsin on peptide chain:

Chymotrypsin helps in breaking down protein into smaller units known as amino acids and cleaves at the carboxyl side of aromatic amino acids such as tyrosine, tryptophan, phenylalanine etc.

Cleavage sites of chymotrypsin

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Most popular questions from this chapter

The following structure is drawn in an unconventional manner.

(a) Label the N terminus and the C terminus.

(b) Label the peptide bonds.

(c) Identify and label each amino acid present.

(d) Give the full name and the abbreviated name

Show how you would synthesize Leu-Gly-Ala-Val-Phe starting with Fmoc-Ala-Val-Phe— P

Draw the electrophoretic separation of Trp, Cys, and His at pH 6.0.

Daw the structure of the predominant form of

Isoleucine at pH 11 (b) Proline at pH 2

Arginine at pH 7 (d) Glutamic acid at pH 7

A mixture of alanine, lysine, and aspartic acid at 1). pH 6 ; 2). pH 11; 3). pH

Draw the resonance forms of a protonated guanidino group and explain why arginine has such a strongly basic isoelectric point.

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