Hao M H, Scheraga H A
Boehringer Ingelheim Pharmaceuticals Inc. R6-5, 900 Ridgebury Road, PO Box 368, Ridgefield, CT 06877, USA.
Curr Opin Struct Biol. 1999 Apr;9(2):184-8. doi: 10.1016/s0959-440x(99)80026-8.
By following a consistent line of physical reasoning, some fundamental understanding about the foldability of proteins has been achieved. In recent years, this has led to the development of a number of successful algorithms for optimizing potential energy functions for folding protein models. The differences between the folding mechanisms of simple, contact-based lattice proteins and more traditional, realistic protein models, however, still call for further development of the potentials in addition to the optimization approaches.
通过遵循一致的物理推理思路,已经获得了一些关于蛋白质可折叠性的基本认识。近年来,这促使开发了许多成功的算法来优化蛋白质折叠模型的势能函数。然而,简单的基于接触的晶格蛋白质与更传统的实际蛋白质模型的折叠机制之间的差异,除了优化方法之外,仍需要进一步开发势能函数。