期刊
PROTEIN SCIENCE
卷 12, 期 9, 页码 2057-2062出版社
WILEY
DOI: 10.1110/ps.0302503
关键词
protein folding kinetics; two-state kinetics; multistate kinetics; contact order; protein size; protein topology; rate of folding
Guided by the recent success of empirical model predicting the folding rates of small two-state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chain length L as L-2/3, and by the finding that the folding rates of multistate folding proteins strongly correlate with their sizes and have very bad correlation with CO, we reexamined the dependence of folding rate on CO and L in attempt to find a structural parameter that determines folding rates for the totality of proteins. We show that the Abs_CO = CO x L, is able to predict rather accurately folding rates for both two-state and multistate folding proteins, as well as short peptides, and that this Abs-CO scales with the protein chain length as L0.70+/-0.07 for the totality of studied single-domain proteins and peptides.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据