Crippen G M, Viswanadhan V N
Int J Pept Protein Res. 1985 May;25(5):487-509. doi: 10.1111/j.1399-3011.1985.tb02203.x.
An improved potential function has been devised for the calculation of protein conformations. Each amino acid residue is represented by two points. The mainchain is traced by the sequence of C alpha atoms, and the details of sidechain structure and interactions are represented by a representative sidechain atom. This potential function has been developed from a data base of 22 high resolution protein crystal structures and includes the components of an earlier potential developed from a similar data base where each amino acid residue is represented by only its C alpha atom. In virtually all aspects of testing, the present potential betters the previous single-point potential, and is shown to be useful in the simulation of protein folding.
已设计出一种改进的势能函数用于计算蛋白质构象。每个氨基酸残基由两个点表示。主链由α碳原子序列追踪，侧链结构和相互作用的细节由一个代表性侧链原子表示。该势能函数是从22个高分辨率蛋白质晶体结构的数据库发展而来的，并且包含了早期从类似数据库发展而来的势能的组成部分，在该早期数据库中每个氨基酸残基仅由其α碳原子表示。在几乎所有测试方面，当前的势能函数都优于先前的单点势能函数，并且已证明其在蛋白质折叠模拟中很有用。
