TOWARD UNDERSTANDING AMYLOIDO ALL-ATOM MOLECULAR DYNAMICS SIMUALTIONS OF AM

理解淀粉样蛋白的全原子分子动力学模拟

• 批准号: 7723171
• 负责人: YONG DUAN
• 金额: $ 0.05万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-08-01 至 2009-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7723171
• 关键词: Computer Retrieval of Information on Scientific Projects Database; Development; Funding; Grant; Institution; Mechanics; Modeling; Plant Roots; Process; Proteins; Research; Research Personnel; Resources; Source; United States National Institutes of Health; molecular dynamics; protein folding; quantum; simulation; villin

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.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 准确模拟折叠过程是全面阐明蛋白质折叠机制的关键一步。我们最近成功地从头开始全原子分子动力学模拟了绒毛头子域 (HP35) 的折叠过程，Ca-RMSD（均方根偏差）小于 0.5，这表明实现高精度蛋白质建模的潜力。我们请求继续支持进一步推进蛋白质折叠机制的高精度建模，并为力场参数的开发进行高水平的量子力学计算。