Development of an ab initio MO-MD program based on fragment MO method - an attempt to analyze the fluctuation of protein

被引：22

作者：

Ishimoto, T

Tokiwa, H

Teramae, H

Nagashima, U

机构：

[1] Natl Inst Adv Ind Sci & Technol, Grid Technol Res Ctr, Tsukuba, Ibaraki 3058561, Japan

[2] Rikkyo Univ, Fac Sci, Dept Chem, Toshima Ku, Tokyo 1718501, Japan

[3] NTT Corp, Basic Res Labs, Atsugi, Kanagawa 2430198, Japan

来源：

CHEMICAL PHYSICS LETTERS | 2004年 / 387卷 / 4-6期

关键词：

D O I：

10.1016/j.cplett.2004.01.105

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

In order to analyze the fluctuation of proteins, which plays an important role for folding structure and stability, an ab initio MO-MD program (FMO-HA) based on the fragment MO method has been developed and examined its efficiency in comparison with conventional RHF MO-MD. FMO gives the same potential of dissociation energy between fragments as well as RHF. FMO-HA and RHF MO-MD calculations show similar trajectories and geometrical changes. Furthermore. FMO-HA simulation enables us to elucidate the interaction energy between fragments accompanying with the dynamics. FMO-HA method is an efficient tool to determine the driving force of fluctuation of proteins. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：460 / 465

页数：6

共 17 条

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*AIST, PEACH VERS 3 8

[2] EVALUATION OF MOLECULAR INTEGRALS OVER GAUSSIAN BASIS FUNCTIONS [J].