Chapter 24: Q28P. (page 1297)
Draw the complete structure of the following peptide Met-Ser-Gln-
Short Answer
Complete structure of the peptide
Chapter 24: Q28P. (page 1297)
Draw the complete structure of the following peptide Met-Ser-Gln-
Complete structure of the peptide
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Get started for freeDraw the electrophoretic separation of Ala, Lys, and Asp at pH 9.7.
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.
Show the steps and intermediates in the synthesis of Leu-Ala-Phe by the solid-phase process.
Although tryptophan contains a heterocyclic amine, it is considered a neutral amino acid. Explain why the indole nitrogen of trytophan is more weakly basic than one of the imidazole nitrogens of histidine.
Lipoic acid is often found near the active sites of enzymes, usually bound to the peptide by a long, flexible amide linkage with a lysine residue.
(a) Is lipoic acid a mild oxidizing agent or a mild reducing agent? Draw it in both its oxidized and reduced forms.
(b) Show how lipoic acid might react with two Cys residues to form a disulfide bridge.
(c) Give a balanced equation for the hypothetical oxidation or reduction, as you predicted in part (a), of an aldehyde by lipoic acid.
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