DETECTION AND CHARACTERIZATION OF A FOLDING INTERMEDIATE IN BARNASE BY NMR

被引：218

作者：

BYCROFT, M ^{[1
]}

MATOUSCHEK, A ^{[1
]}

KELLIS, JT ^{[1
]}

SERRANO, L ^{[1
]}

FERSHT, AR ^{[1
]}

机构：

[1] UNIV CAMBRIDGE,DEPT CHEM,MRC,PROT FUNCT & DESIGN UNIT,CAMBRIDGE CB2 1EW,ENGLAND

来源：

NATURE | 1990年 / 346卷 / 6283期

关键词：

D O I：

10.1038/346488a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

PROTEIN engineering is being developed for mapping the energetics and pathway of protein folding. From kinetic studies on wild-type and mutant proteins, the sequence and energetics of formation of tertiary interactions of side chains can be mapped and the formation of secondary structure inferred1,2. Here we cross-check and complement results from this approach by using a recently developed procedure that traps and characterizes secondary structure in intermediate states using 1H NMR3,4. The refolding of barnase is shown to be a multiphasic process in which the secondary structure in α-helices and β-sheets and some turns is formed more rapidly than is the overall folding. © 1990 Nature Publishing Group.

引用

页码：488 / 490

页数：3

共 8 条

[1]

BYCROFT M, IN PRESS BIOCHEMISTR

[2] DEMONSTRATION OF 2 REACTION PATHWAYS FOR AMINOACYLATION OF TRANSFER-RNA - APPLICATION OF PULSED QUENCHED FLOW TECHNIQUE [J].