Synthesis, conformation and reactivity towards p‐nitrophenyl acetate of polypeptides incorporating aspartic acid, serine and histidine
- 1 May 1982
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 19 (5) , 528-535
- https://doi.org/10.1111/j.1399-3011.1982.tb02638.x
Abstract
Examination of .beta.-carbon coordinates of seryl, aspartyl and histidyl residues in active sites of .alpha.-chymotrypsin and subtilisin BPN'' shows tha a close geometrical arrangement can be obtained in an antiparallel .beta.-structure. Therefore some polypeptides incorporating serine, aspartic acid and histidine, poly (Gly-Ser-Asp-His-Ala-Pro) and poly [(Asp-Leu-Asp-Leu)10, (His-Leu-Ser-Leu)1], and expected to have some tendency to give rise to an antiparallel .beta.-conformation, were prepared and studied. The second polymer only adopts a fairly well-defined .beta.-structure in aqueous solution. Catalytic activities of these products towards p-nitrophenyl acetate are not improved as compared to histidine. However, kinetic pK of histidine side-chain depends markedly upon the nature of the product, owing probably to a hydrophobic environment effect.Keywords
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