期刊
JOURNAL OF COMPUTATIONAL CHEMISTRY
卷 22, 期 12, 页码 1229-1242出版社
JOHN WILEY & SONS INC
DOI: 10.1002/jcc.1080
关键词
proteins; reduced models; protein structure prediction; force fields; molecular dynamics
Parameterization and test calculations of a reduced protein model with new energy terms are presented. The new energy terms retain the steric properties and the most significant degrees of freedom of protein side chains in an efficient way using only one to three virtual atoms per amino acid residue. The energy terms are implemented in a force field containing predefined secondary structure elements as constraints, electrostatic interaction terms, and a solvent-accessible surface area term to include the effect of solvation. In the force field the main-chain peptide units are modeled as electric dipoles, which have constant directions in alpha -helices and beta -sheets and variable conformation-dependent directions in loops. Protein secondary structures can be readily modeled using these dipole terms. Parameters of the force field were derived using a large set of experimental protein structures and refined by minimizing RMS errors between the experimental structures and structures generated using molecular dynamics simulations. The final average RMS error was 3.7 Angstrom for the main-chain virtual atoms (C-alpha atoms) and 4.2 Angstrom for all virtual atoms for a test set of 10 proteins with 58-294 an-Lino acid residues. The force field was further tested with a substantially larger test set of 608 proteins yielding somewhat lower accuracy. The fold recognition capabilities of the force field were also evaluated using a set of 27,814 misfolded decoy structures. (C) 2001 John Wiley & Sons, Inc.
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