Engineering of zinc finger and MHC motifs to locked-in tertiary folds

被引：0

作者：

Mathieu, M ^{[1
]}

Lehmann, C ^{[1
]}

Razaname, A ^{[1
]}

Tuchscherer, G ^{[1
]}

机构：

[1] UNIV LAUSANNE,INST ORGAN CHEM,BCH DORIGNY,CH-1015 LAUSANNE,SWITZERLAND

来源：

LETTERS IN PEPTIDE SCIENCE | 1997年 / 4卷 / 02期

关键词：

protein design; locked-in folds; chemoselective ligation; zinc finger motif; MHC motif; protein mimetics; non-native architectures;

D O I：

暂无

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：

The assembly of helical and beta-sheet peptide blocks containing reactive chain ends results in highly branched chain architectures ('locked-in folds') mimicking native tertiary structures. This molecular kit strategy allows to bypass the protein folding problem in protein de novo design and gives access to protein mimetics of high thermodynamic stability. The validity of this concept is exemplified for the design and synthesis of locked-in folds mimicking the zinc finger and MWC folding motifs.

引用

页码：95 / 100

页数：6

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