Optimization of the loop length for folding of a helix-loop-helix peptide

被引：33
|
作者：
Suzuki, N [1 ]
Fujii, N [1 ]
机构：
[1] Biomol Engn Res Inst, Osaka 5650874, Japan
来源：
TETRAHEDRON LETTERS | 1999年 / 40卷 / 33期
关键词：
peptides; polypeptides; structure-activity; circular dichroism; helices;
D O I：
10.1016/S0040-4039(99)01095-3
中图分类号：
O62 [有机化学];
学科分类号：
070303 ; 081704 ;
摘要：
We have designed and synthesized compact helix-loop-helix peptides as a scaffold for conformationally defined peptide mimetics. Circular dichroism and sedimentation equilibrium studies suggested that the connection between the two helical segments significantly affected the structural formation. The loop length corresponding to seven glycine residues (approximately 25 Angstrom) was found to be most suitable for the intrachain packing of the oc-helices. (C) 1999 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码：6013 / 6017
页数：5
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