Zwanzig R
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Proc Natl Acad Sci U S A. 1997 Jan 7;94(1):148-50. doi: 10.1073/pnas.94.1.148.
The folding of some proteins appears to be a two-state kinetic process. A two-state kinetic model is justified if protein molecules rapidly equilibrate between different unfolded conformations prior to complete folding. Here I show that this rapid equilibration is a natural consequence of reasonable assumptions about reaction rate constants and folding thermodynamics.
一些蛋白质的折叠似乎是一个两态动力学过程。如果蛋白质分子在完全折叠之前能在不同的未折叠构象之间迅速达到平衡,那么两态动力学模型就是合理的。在此我表明,这种快速平衡是关于反应速率常数和折叠热力学的合理假设的自然结果。