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
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
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Get started for freeShow how solid-phase peptide synthesis would be used to make Ile-Gly-Asn.
Show how the following amino acids might be formed in the laboratory by reductive amination of the appropriate -ketoacid.
Phenylalanine (b) Cysteine (c) Serine (d) Alanine
Show how you would use a Strecker synthesis to make
Answer
Give equations for the formation and hydrogenolysis of the glutamine benzyl ester
The Sanger method for N-terminus determination is a less common alternative to the Edman degradation. In the Sanger method, the peptide is treated with the Sanger reagent, 2,4-dinitrofluorobenzene, and then hydrolyzed by reaction with 6 M aqueous HCl. The N-terminal amino acid is recovered as its 2,4-dinitrophenyl derivative and identified.
(a)Propose a mechanism for the reaction of the N terminus of the peptide with 2,4-dinitrofluorobenzene.
(b) Explain why the Edman degradation is usually preferred over the Sanger method.
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