10 residue folded peptide designed by segment statistics

被引:261
作者
Honda, S [1 ]
Yamasaki, K [1 ]
Sawada, Y [1 ]
Morii, H [1 ]
机构
[1] Natl Inst Adv Ind Sci & Technol, Tsukuba, Ibaraki 3058566, Japan
关键词
D O I
10.1016/j.str.2004.05.022
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have designed a peptide termed chignolin, consisting of only 10 amino acid residues (GYDPETGTWG), on the basis of statistics derived from more than 10,000 protein segments. The peptide folds into a unique structure in water and shows a cooperative thermal transition, both of which may be hallmarks of a protein. Also, the experimentally determined beta-hairpin structure was very close to what we had targeted. The performance of the short peptide not only implies that the methodology employed here can contribute toward development of novel techniques for protein design, but it also yields insights into the raison d'etre of an autonomous element involved in a natural protein. This is of interest for the pursuit of folding mechanisms and evolutionary processes of proteins.
引用
收藏
页码:1507 / 1518
页数:12
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