蛋白质动力学粗粒化模型中的别构效应
生物大分子
2009-09-29 v7
摘要
我们提出蛋白质粗粒化模型中参数选择的优化准则，并发展了牛胰蛋白酶原的精细化弹性网络模型（ENM）。胰蛋白酶原ENM的单峰态密度分布与全原子模型所得双峰分布不一致；然而，通过增强骨架相邻原子间的相互作用可恢复双峰分布。我们利用骨架增强模型分析胰蛋白酶原的别构机制，发现调控位点与活性位点间存在较强的通讯。
引用
@article{arxiv.q-bio/0506031,
title = {Allostery in a Coarse-Grained Model of Protein Dynamics},
author = {Dengming Ming and Michael Wall},
journal= {arXiv preprint arXiv:q-bio/0506031},
year = {2009}
}
备注
11 pages, 3 figures; Fixed typo in Eq. (4); Changed local report number; Renormalized Fig. 1 to # of non-zero modes; Fixed scales of MSDs in Fig. 2; shortened manuscript; changed author list; fixed error in reference to active and regulatory sites of trypsinogen; added journal reference and DOI