Chapter 21: Q32P (page 1010)
What dipeptides would be formed by heating a mixture of valine and N- protected leucine?
Short Answer
The answer is:
Leu-Val
Val-Val
Chapter 21: Q32P (page 1010)
What dipeptides would be formed by heating a mixture of valine and N- protected leucine?
The answer is:
Leu-Val
Val-Val
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Get started for freeAfter the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride,
trypsin will cleave the polypeptide only on the C-side of arginine.)
Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-
Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp
a. After a polypeptide is treated with maleic anhydride, why does trypsin no longer cleave it on the C-side of lysine?
b. How many fragments are obtained from the polypeptide?
c. In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?
Explain the difference in the \({\bf{p}}{{\bf{K}}_{\bf{a}}}\) values of the carboxyl groups of alanine, serine, and cysteine.
Show the peptides that would result from cleavage by the indicated reagent:
a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A
b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide
c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsin
A mixture of amino acids that do not separate sufficiently when a single technique is used can often be separated by two-dimensional chromatography.In this technique, the mixture of amino acids is applied to a piece of filter paper and separated by chromatographic techniques. The paper is then rotated90°,and the amino acids are further separated by electrophoresis, producing a type of chromatogram called a fingerprint.Identify the spots in the fingerprint obtainedfrom a mixture of Ser, Glu, Leu, His, Met, and Thr.
What alkyl halide is used in the acetamidomalonic ester synthesis to prepare a. lysine? b. phenylalanine?
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