Zwanzig R
Laboratory of Chemical Physics, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9801-4. doi: 10.1073/pnas.92.21.9801.
A simple model of the kinetics of protein folding is presented. The reaction coordinate is the "correctness" of a configuration compared with the native state. The model has a gap in the energy spectrum, a large configurational entropy, a free energy barrier between folded and partially folded states, and a good thermodynamic folding transition. Folding kinetics is described by a master equation. The folding time is estimated by means of a local thermodynamic equilibrium assumption and then is calculated both numerically and analytically by solving the master equation. The folding time has a maximum near the folding transition temperature and can have a minimum at a lower temperature.
提出了一个蛋白质折叠动力学的简单模型。反应坐标是与天然状态相比的一种构象的“正确性”。该模型在能谱中有一个间隙、一个大的构型熵、折叠态和部分折叠态之间的自由能垒以及一个良好的热力学折叠转变。折叠动力学由主方程描述。通过局部热力学平衡假设估计折叠时间，然后通过求解主方程进行数值和解析计算。折叠时间在折叠转变温度附近有一个最大值，并且在较低温度下可能有一个最小值。
