CHARACTERIZING TRANSITION-STATES IN PROTEIN-FOLDING - AN ESSENTIAL STEP IN THE PUZZLE

被引:279
作者
FERSHT, AR
机构
基金
英国医学研究理事会;
关键词
D O I
10.1016/0959-440X(95)80012-P
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
Transition states in protein folding are being analyzed experimentally and by computer simulation to reveal the sequence of events in the folding and unfolding of proteins at high resolution. Results of this analysis have enabled the reconstruction of folding pathways in vitro and open the prospect of analyzing pathways in vivo.
引用
收藏
页码:79 / 84
页数:6
相关论文
共 26 条
[21]  
MATOUSCHEK A, 1991, METHOD ENZYMOL, V202, P81
[22]   STRUCTURE OF THE TRANSITION-STATE FOR THE FOLDING/UNFOLDING OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 AND ITS IMPLICATIONS FOR MECHANISMS OF PROTEIN-FOLDING [J].
OTZEN, DE ;
ITZHAKI, LS ;
ELMASRY, NF ;
JACKSON, SE ;
FERSHT, AR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (22) :10422-10425
[23]  
RODER H, 1988, NATURE, V335, P694
[24]   HOW DOES A PROTEIN FOLD [J].
SALI, A ;
SHAKHNOVICH, E ;
KARPLUS, M .
NATURE, 1994, 369 (6477) :248-251
[25]   THE FOLDING OF AN ENZYME .3. STRUCTURE OF THE TRANSITION-STATE FOR UNFOLDING OF BARNASE ANALYZED BY A PROTEIN ENGINEERING PROCEDURE [J].
SERRANO, L ;
MATOUSCHEK, A ;
FERSHT, AR .
JOURNAL OF MOLECULAR BIOLOGY, 1992, 224 (03) :805-818
[26]  
UDGAONKAR JB, 1988, NATURE, V335, P700