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 tripeptides Gly–Ala–Ser and Ala–Ser–Arg.

Deduce the sequence of a pentapeptide that contains the amino acids Ala, Glu, Gly, Ser, and Tyr, from the following experimental data. Edman degradation cleaves Gly from the pentapeptide, and carboxypeptidase forms Ala and a tetrapeptide. Treatment of the pentapeptide with chymotrypsin forms a dipeptide and a tripeptide. Partial hydrolysis forms Gly, Ser, and the tripeptide Tyr–Glu–Ala.

What peptides are expected to be produced when a-melanotropin (Problem 2) is cleaved by (a) trypsin, (b) cyanogen bromide, and (c) thermolysin?

Hydrolysis of decapeptide P with the enzyme trypsin affords the following fragments: Gly-Asp, Ala-Cys-Lys, Leu-Trp- Val-Gly-Arg. Hydrolysis with chymotrypsin yields: Leu-Trp, Val-Gly-Arg-Ala-Cys-Lys-Gly-Asp. What is the amino acid sequence of P?

Determine the primary structure of an octapeptide from the following data: Acid-catalyzed hydrolysis gives 2 Arg, Leu, Lys, Met, Phe, Ser, and Tyr. Carboxypeptidase A releases Ser. Edman’s reagent releases Leu. Treatment with cyanogen bromide forms two peptides with the following amino acid compositions: 1. Arg, Phe, Ser 2. Arg, Leu, Lys, Met, Tyr Trypsin-catalyzed hydrolysis forms the following two amino acids and two peptides: 1. Arg 2. Ser 3. Arg, Met, Phe 4. Leu, Lys, Tyr

Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below,  please show them in zig-zag style, from amino to carboxy terminus, with correct  stereochemistry please highlight the part has been change Draw the predominant form at pH = 2  Draw the predominant form at pH = 5  Draw the predominant form at pH = 7  Draw the predominant form at pH = 12

Which of these dipeptides are hydrolyzed by trypsin? by chymotrypsin? Q.) Phe-Gly-Lys

A decapeptide has the following amino acid composition. Ala2, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides. Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala + Lys-Val-Phe + Val-Phe-Gly One round of Edman degradation yields a lysine phenylthiohydantoin. From this information, deduce the primary structure of this decapeptide.

5) Identify each of the following observations about protein or 4' structure A. Amino acids 14-38 in the sequence are arranged in structure as being aspects of the 1', 2', 3', a-helix pattern. B. When the protein was enzymatically broken apart, one of the fragments was found to be Ala-Lys. C. The entire molecule is globular 1.3 times as long in Leu-Tyr-Gly- one dimension as its diameter. D. Detergent was added to a water solution of the protein. The molecular weight study before the addition indicated a single protein with a molecular weight of 150,000. After the addition, two proteins were present with molecular weights 25,000 and 50,000.

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