Polypeptide helices in hybrid peptide sequences

被引:77
作者
Ananda, K
Vasudev, PG
Sengupta, A
Raja, KMP
Shamala, N [1 ]
Balaram, P
机构
[1] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India
[2] Indian Inst Sci, Dept Phys, Bangalore 560012, Karnataka, India
关键词
D O I
10.1021/ja055799z
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A new class of polypeptide helices in hybrid sequences containing alpha-, beta-, and gamma-residues is described. The molecular conformations in crystals determined for the synthetic peptides Boc-Leu-Phe-Val-Aib-beta Phe-Leu-Phe-Val-OMe 1 (beta Phe: (S)-beta(3)-homophenylalanine) and Boc-Aib-Gpn-Aib-Gpn-OMe 2 (Gpn: 1-(aminomethyl)cyclohexaneacetic acid) reveal expanded helical turns in the hybrid sequences (alpha alpha beta)(n) and (ay), In 1, a repetitive helical structure composed Of C-14 hydrogen-bonded units is observed, whereas 2 provides an example of a repetitive C-12 hydrogen-bonded structure. Using experimentally determined backbone torsion angles for the hydrogen-bonded units formed by hybrid sequences, we have generated energetically favorable hybrid helices. Conformational parameters are provided for C-11, C-12, C-13, C-14, and C-15 helices in hybrid sequences.
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页码:16668 / 16674
页数:7
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