Modeling protein association mechanisms and kinetics.
Modeling protein association mechanisms and kinetics.
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DOI：
10.1016/j.sbi.2013.06.014
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发表时间：
2013-12
影响因子：
6.8
通讯作者：
Bates PA
中科院分区：
文献类型：
--
作者：
Zhou HX;Bates PA
在蛋白质缔合机理的建模和缔合速率常数（ka）的计算方面取得了很大的进展。我们现在已经清楚地了解了大范围实验ka值背后的物理因素。一半的关联问题，其中卡是有限的扩散，也许是解决，和另一半，构象变化成为限速，一些有前途的方法正在开发的ka计算。值得注意的是，无序蛋白质的结合动力学正受到越来越多的关注，“对接和聚结”成为一种通用机制。在模拟细胞的异质性、拥挤环境的条件下，蛋白质缔合动力学的建模也取得了进展，这一奋进最终将导致更好地理解细胞功能。
Substantial advances have been made in modeling protein association mechanisms and in calculating association rate constants (ka). We now have a clear understanding of the physical factors underlying the wide range of experimental ka values. Half of the association problem, where ka is limited by diffusion, is perhaps solved, and for the other half, where conformational changes become rate-limiting, a number of promising methods are being developed for ka calculations. Notably, the binding kinetics of disordered proteins are receiving growing attention, with “dock-and-coalescence” emerging as a general mechanism. Progress too has been made in the modeling of protein association kinetics under conditions mimicking the heterogeneous, crowded environments of cells, an endeavor that should ultimately lead to a better understanding of cellular functions.
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影响因子：
2.9
作者：
Myles, T;Le Bonniec, BF;Stone, SR
通讯作者：
Stone, SR
DOI：
10.1073/pnas.89.8.3338
发表时间：
1992-04-15
影响因子：
11.1
作者：
NORTHRUP, SH;ERICKSON, HP
通讯作者：
ERICKSON, HP
影响因子：
3.5
作者：
GOLDBERG, ME;SEMISOTNOV, GV;SUGAI, S
通讯作者：
SUGAI, S
影响因子：
7.3
作者：
Kiel, Christina;Serrano, Luis
通讯作者：
Serrano, Luis
影响因子：
4.3
作者：
Moal, Iain H.;Bates, Paul A.
通讯作者：
Bates, Paul A.