Estimation of protein folding probability from equilibrium simulations

被引：33

作者：

Rao, F ^{[1
]}

Settanni, G ^{[1
]}

Guarnera, E ^{[1
]}

Caflisch, A ^{[1
]}

机构：

[1] Univ Zurich, Dept Biochem, CH-8057 Zurich, Switzerland

来源：

JOURNAL OF CHEMICAL PHYSICS | 2005年 / 122卷 / 18期

关键词：

D O I：

10.1063/1.1893753

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：

The assumption that similar structures have similar folding probabilities (p(fold)) leads naturally to a procedure to evaluate p(fold) for every snapshot saved along an equilibrium folding-unfolding trajectory of a structured peptide or protein. The procedure utilizes a structurally homogeneous clustering and does not require any additional simulation. It can be used to detect multiple folding pathways as shown for a three-stranded antiparallel beta-sheet peptide investigated by implicit solvent molecular dynamics simulations. (c) 2005 American Institute of Physics.

引用

页数：5

共 21 条

[1]

Beck C., 1993, THERMODYNAMICS CHAOT

[2] CHARMM - A PROGRAM FOR MACROMOLECULAR ENERGY, MINIMIZATION, AND DYNAMICS CALCULATIONS [J].