Protein folding: Thickening the broth

被引:50
作者
Minton, AP [1 ]
机构
[1] NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1016/S0960-9822(00)00301-8
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
Recent results support the notion that macromolecular 'crowding' enhances protein aggregation, at the expense of correct folding. The results can be rationalised in terms of kinetic competition between distinct processes, taking into account the relative influence of crowding on each process.
引用
收藏
页码:R97 / R99
页数:3
相关论文
共 15 条
[11]   THE FOLDING OF HEN LYSOZYME INVOLVES PARTIALLY STRUCTURED INTERMEDIATES AND MULTIPLE PATHWAYS [J].
RADFORD, SE ;
DOBSON, CM ;
EVANS, PA .
NATURE, 1992, 358 (6384) :302-307
[12]   Chaperonin function: Folding by forced unfolding [J].
Shtilerman, M ;
Lorimer, GH ;
Englander, SW .
SCIENCE, 1999, 284 (5415) :822-825
[13]   Effects of macromolecular crowding on protein folding and aggregation [J].
van den Berg, B ;
Ellis, RJ ;
Dobson, CM .
EMBO JOURNAL, 1999, 18 (24) :6927-6933
[14]   The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase [J].
van den Berg, P ;
Chung, EW ;
Robinson, CV ;
Mateo, PL ;
Dobson, CM .
EMBO JOURNAL, 1999, 18 (17) :4794-4803
[15]   MACROMOLECULAR CROWDING - BIOCHEMICAL, BIOPHYSICAL, AND PHYSIOLOGICAL CONSEQUENCES [J].
ZIMMERMAN, SB ;
MINTON, AP .
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1993, 22 :27-65