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Sagot :
We have a few reactions we can employ to figure out a polypeptide's sequence. The N-terminal amino acid can be identified using Edman's reagent.
The C-terminal amino acid can then be identified using carboxypeptidase A. The C-side of Met and trypsin, as well as the C-side of Arg and Lys, are both hydrolyzed by cyanogen bromide.
a. There are two alternative sequences for the fragments of polypeptide I: Val-Gly-Asp-Lys-Leu-Glu-Pro-Ala-Arg-Ala-Leu-Gly-Asp and Leu-Glu-Pro-Ala-Arg-Val-Gly-Asp-Lys-Ala-Leu-Gly-Asp. Depending on whether Leu or Val is released, Edman's reagent can reveal the
b. The sequences for the polypeptide II fragments are: Ala-Glu-Pro-Arg-Ala-Met-Gly-Lys-Val-Leu-Gly-Glu and Ala-Met-Gly-Lys-Ala-Glu-Pro-Arg-Ala-Met-Gly-Lys-Val-Leu-Gly-Glu. Cyanogen bromide can be used to determine the actual sequence. The initial segment would be split up into a one into two hexamers, the other into a dimer and decamer.
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complete question : Three peptides were obtained from a trypsin digestion of two different polypeptides. In each case, indicate the possible sequences from the given data and tell what further experiment should be carried out in order to determine the primary structure of the polypeptide. a. polypeptide I: 1. Val-Gly-Asp-Lys 2. Leu-Glu-Pro-Ala-Arg 3. Ala-Leu-Gly-Asp; b. polypeptide II: 1. Val-Leu-Gly-Glu 2. Ala-Glu-Pro-Arg 3. Ala-Met-Gly-Lys
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