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  • Title: Synthesis, conformation and reactivity towards p-nitrophenyl acetate of polypeptides incorporating aspartic acid, serine and histidine.
    Author: Trudelle Y.
    Journal: Int J Pept Protein Res; 1982 May; 19(5):528-35. PubMed ID: 6811470.
    Abstract:
    Examination of beta-carbons coordinates of seryl, aspartyl and histidyl residues in active sites of alpha-chymotrypsin and subtilisin BPN' shows that a close geometrical arrangement can be obtained in an antiparellel 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, have been 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.
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