TOWARD UNDERSTANDING AMYLOIDO ALL-ATOM MOLECULAR DYNAMICS SIMUALTIONS OF AM

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 对折叠过程的准确模拟是全面阐明蛋白质折叠机制的关键一步。我们最近成功的从头算全原子分子动力学模拟了Villin头饰亚域(HP35)的折叠过程，使其均方根偏差(RMSD)小于0.5，这表明有可能实现高精度的蛋白质建模。我们要求继续支持进一步推进蛋白质折叠机制的高精度建模，并执行用于开发力场参数的高级量子力学计算。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Accurate simulation of the folding processes is a crucial step toward a full elucidation of the mechanisms of protein folding. Our recent successful ab initio all-atom molecular dynamics simulations of the folding processes of villin headpiece subdomain (HP35) to a Ca-RMSD (root-mean-square-deviation) of less than 0.5 indicates the potential to achieve high-accuracy protein modeling. We request continued support to further advancement toward highly accurate modeling of the protein folding mechanisms and to perform high-level quantum mechanical calculations for the development of the force field parameters.