Jernigan R L, Bahar I
Laboratory of Mathematical Biology, National Institutes of Health, Bethesda, MD 20892-5677, USA.
Curr Opin Struct Biol. 1996 Apr;6(2):195-209. doi: 10.1016/s0959-440x(96)80075-3.
There has recently been an explosion in the number of structure-derived potential functions that are based on the increasing number of high-resolution protein crystal structures. These functions differ principally in their reference states; the usual two classes correspond either to initial solvent exposure or to residue exposure of residues. Reference states are critically important for applications of these potentials functions. Inspection of the potential functions and their derivation can tell us not only about protein interaction strengths themselves, but can also provide suggestions for the design of better folding simulations. An appropriate goal in this field is achieving self-consistency between the details in the derivation of potentials and the applied simulations.
最近，基于越来越多的高分辨率蛋白质晶体结构的结构衍生势函数数量激增。这些函数的主要区别在于其参考状态；通常的两类分别对应于初始溶剂暴露或残基的残基暴露。参考状态对于这些势函数的应用至关重要。对势函数及其推导的研究不仅可以告诉我们蛋白质相互作用强度本身，还可以为更好的折叠模拟设计提供建议。该领域的一个合适目标是在势的推导细节与应用模拟之间实现自洽。
