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
Short Answer

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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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Show how solid-phase peptide synthesis would be used to make Ile-Gly-Asn.
Draw the structure of the predominant form of
(a)Isoleucine at pH 11 (b) Proline at pH 2
(c)Arginine at pH 7 (d) Glutamic acid at pH 7
A mixture of alanine, lysine, and aspartic acid at 1). pH 6 ; 2). pH 11; 3). pH 2
Histidine is an important catalytic residue found at the active sites of many enzymes. In many cases, histidine appears to remove protons or to transfer protons from one location to another.
(a) Show which nitrogen atom of the histidine heterocycle is basic and which is not.
(b) Use resonance forms to show why the protonated form of histidine is a particularly stable cation.
(c) Show the structure that results when histidine accepts a proton on the basic nitrogen of the heterocycle and then is deprotonated on the other heterocyclic nitrogen. Explain how histidine might function as a pipeline to transfer protons between sites within an enzyme and its substrate.
Draw the electrophoretic separation of Trp, Cys, and His at pH 6.0.
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