Observation of strange kinetics in protein folding
Observation of strange kinetics in protein folding
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DOI：
10.1073/pnas.96.11.6031
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发表时间：
1999-05-25
影响因子：
11.1
通讯作者：
Gruebele, M
中科院分区：
文献类型：
--
作者：
Sabelko, J;Ervin, J;Gruebele, M
在温度跳跃诱导的两种蛋白质，酵母磷酸甘油酸激酶和一个泛素突变体的重折叠过程中，观察到了水溶液中的高度非指数折叠动力学。这些观察结果最容易用下坡褶皱来解释，它假定了在通往褶皱状态的过程中存在一个不同种类的结构集合。这些数据也与在不同实验条件下测得的指数动力学以及表明合作折叠的滴定实验相一致。
Highly nonexponential folding kinetics in aqueous solution have been observed during temperature jump-induced refolding of two proteins, yeast phosphoglycerate kinase and a ubiquitin mutant. The observations are most easily interpreted in terms of downhill folding, which posits a heterogeneous ensemble of structures en route to the folded state. The data are also reconciled with exponential kinetics measured under different experimental conditions and with titration experiments indicating cooperative folding.