Qiu Linlin, Hagen Stephen J
Physics Department, University of Florida, P.O. Box 118440, Gainesville Florida 32611-8440, USA.
J Am Chem Soc. 2004 Mar 24;126(11):3398-9. doi: 10.1021/ja049966r.
Because protein folding dynamics are heavily overdamped, Kramers theory predicts the rate of folding to scale inversely with the reaction friction, which is usually interpreted to mean the solvent viscosity. This does not mean, however, that the speed of folding can increase without limit as solvent viscosity decreases. We show that, in a sufficiently fast-folding protein, the folding speed approaches a finite limit at low solvent viscosity, indicating a reaction controlled by internal friction.
由于蛋白质折叠动力学存在严重的过阻尼现象，克莱默斯理论预测折叠速率与反应摩擦力成反比，反应摩擦力通常被理解为溶剂粘度。然而，这并不意味着随着溶剂粘度降低，折叠速度可以无限制地增加。我们表明，在折叠速度足够快的蛋白质中，在低溶剂粘度下折叠速度接近一个有限的极限，这表明反应受内摩擦力控制。
