METASTABILITY OF THE FOLDED STATES OF GLOBULAR-PROTEINS

被引：288
作者：
HONEYCUTT, JD
THIRUMALAI, D
机构：
[1] Dept. of Chemistry and Biochemistry, University of Maryland, College Park
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1990年 / 87卷 / 09期
关键词：
D O I：
10.1073/pnas.87.9.3526
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：
The possibility that several metastable minima exist in which the folded forms of a polypeptide chain have similar structural characteristics but different energies is suggested. The validity of this hypothesis is illustrated with the aid of simulation methods on a model protein that folds into a β-barrel structure. Some implications of this hypothesis such as the existence of multiple pathways with intermediates for protein folding are discussed.
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页码：3526 / 3529
页数：4
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