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: 8364238
• 负责人: YONG DUAN
• 金额: $ 0.11万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-09-15 至 2013-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8364238
• 关键词: Biomedical Research; Development; Funding; Grant; High Performance Computing; Mechanics; Modeling; National Center for Research Resources; Plant Roots; Principal Investigator; Process; Proteins; Research; Research Infrastructure; Resources; Source; United States National Institutes of Health; cost; 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 对折叠过程的准确模拟是朝着全面阐明蛋白质折叠机理的关键步骤。我们最近成功的AB从头算全部原子分子动力学模拟了Villin头次域（HP35）至CA-RMSD（root-mean-square-deviation）的折叠过程，该过程小于0.5，这表明有可能实现高准确蛋白质建模的潜力。我们要求持续支持，以进一步发展蛋白质折叠机制的高度准确建模，并对力场参数的开发进行高级量子机械计算。