Evidence for barrier-limited protein folding kinetics on the microsecond time scale
Evidence for barrier-limited protein folding kinetics on the microsecond time scale
复制标题
微秒时间尺度上屏障限制的蛋白质折叠动力学的证据
DOI:
10.1038/nsb0598-385
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发表时间:
1998
期刊:
影响因子:
--
通讯作者:
H. Roder
中科院分区:
文献类型:
--
作者:
M. Shastry;H. Roder
Although important structural events in protein folding are known to occur on the submillisecond time scale, the limited time resolution of conventional kinetic methods has precluded direct observation of the initial collapse of the polypeptide chain. A continuous-flow capillary mixing method recently developed by us made it possible to account for the entire fluorescence change associated with refolding of cytochrome c from ∼5–10-5-102 s, including the previously unresolved quenching of Trp 59 fluorescence (burst phase) indicative of the formation of compact states. The kinetics of folding exhibits a major exponential process with a time constant of ∼50 μs, independent of initial conditions and heme ligation state, indicating that a common free energy barrier is encountered during the initial collapse of the polypeptide chain. The resulting loosely packed intermediate accumulates prior to the rate-limiting formation of specific tertiary interactions, confirming previous indications that folding involves at least two distinct stages.
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DOI:
10.1073/pnas.94.5.1779
发表时间:
1997-03-04
影响因子:
11.1
作者:
Chan, CK;Hu, Y;Hofrichter, J
通讯作者:
Hofrichter, J
DOI:
10.1021/bi961976k
发表时间:
1996
期刊:
Biochemistry.
影响因子:
--
作者:
Sauder,JM;MacKenzie,NE;Roder,H
通讯作者:
Roder,H
影响因子:
56.9
作者:
JENNINGS, PA;WRIGHT, PE
通讯作者:
WRIGHT, PE
影响因子:
2.9
作者:
Ridge,JA;Baldwin,RL;Labhardt,AM
通讯作者:
Labhardt,AM
影响因子:
--
作者:
Roder,H
通讯作者:
Roder,H