uretups-//sessiöh.masteringchemistry.com/myctyitemView assignmentProblemlD 10112

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uretups-//sessiöh.masteringchemistry.com/myctyitemView assignmentProblemlD 101128241 Protein Structure and Classification oblem 18.32 16 of 37 Part A Trypsin is an endoprotease and it hydrolyzes peptide bonds on the carboxyl side of lysine and arginine. If the following peptide sequence is hydrolyzed by trypsin, how many fragments will there be? Leu-Phe-Arg-Leu-Phe-Cys-Gly-Lys-Ala-Asp-Trp-Ala Check all that apply Ala-Asp-Trp-Ala Arg-Leu-Phe-Cys-Gly Leu-Phe Leu-Phe-Arg O Leu-Phe-Cys-Gly-Lys 2 Lys-Ala-Asp-Trp-Ala Submit vious Answers Request Answer X Incorrect: Trv Aaain: 5 attemots remainina 10:44 AM 4/14/2016 q) 1

Explanation / Answer

Ans> By convention a protein is written with its amino acids from n terminal to the left most side to c terminal at tthe rightmost side. So the N to C terminal of the given amino acid is: Leu-Phe-Arg-Leu-Phe-Cys-Gly-Lys-Ala-Asp-Trp-Ala.

Now trypsin hydrolyses lysine and argenine peptide bond on the carboxyl side. So there will be three fragments generated: Leu-Phe-Arg ; Leu-Phe-Cys-Gly-Lys ; Ala-Asp-Trp-Ala  

As trypsin hydrolyses the carboxyl end so it cleaves the peptide bond on the right side of argenine and lysine.

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