期刊
JOURNAL OF MECHANICAL DESIGN
卷 127, 期 4, 页码 712-717出版社
ASME-AMER SOC MECHANICAL ENG
DOI: 10.1115/1.1867502
关键词
-
This paper presents an efficient and novel computational protein prediction methodology called kineto-static compliance method. Successive kineto-static fold compliance is a methodology for predicting a protein molecule's motion under the effect of an interatomic force field without the need for molecular-dynamic simulation. Instead, the chain complies under the kineto-static effect of the force field in such a manner that each rotatable joint changes by an amount proportional to the effective torque on that joint. This process successively iterates until all of the joint torques have converged to a minimum. This configuration is equivalent to a stable, globally optimized potential energy state of the system or in other words, the final conformation of the protein. This methodology is implemented in a computer software package named PROTOFOLD. In this paper we have used PROTOFOLD to predict the final conformation of a small peptide chain segment, an alpha helix, and the Triponin protein chains from a denatured configuration. The results show that torques in each joint are minimized to values very close to zero, which demonstrates the method's effectiveness for protein conformation prediction.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据