MODELING PROTEIN STRUCTURE USING SPARSE NMR CONSTRAINTS

使用稀疏 NMR 约束对蛋白质结构进行建模

• 批准号: 8361793
• 负责人: JAMES H. PRESTEGARD
• 金额: $ 0.18万
• 依托单位: UNIVERSITY OF GEORGIA
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-02-01 至 2012-01-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361793
• 关键词: Cell surface; Coupling; Data; Funding; Goals; Grant; Homology Modeling; Methods; Modeling; National Center for Research Resources; Oligosaccharides; Principal Investigator; Proteins; Research; Research Infrastructure; Residual state; Resources; Source; Structure; United States National Institutes of Health; Universities; Washington; Work; cost; design; glycosyltransferase; improved; programs; protein structure; restraint

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. It has been difficult to obtain experimental structural information on many of the proteins important in the synthesis of cell-surface oligosaccharides (glycosyltransferases, for example). Yet, many of these proteins show strong hits from computational threading programs, some structures can be homology modeled, and others can be predicted from well designed force fields. The goal of this project is to explore the use of residual dipolar coupling (RDC) restraints and paramagnetic distance restraints in improving the efficiency of searches and the quality of the structures that result. The Research Resource will be providing RDC and distance data on model proteins, as well as glycosyltransferases, to the computational groups such as the Baker group at the University of Washington, so that they can modify their approaches to accommodate the inclusion of these types of NMR data. The goal is to develop methods for structure determination that can work with challenging proteins for which only limited amounts of structural data can be obtained.

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。 很难获得有关许多在合成细胞表面寡糖（例如，糖基转移酶）中重要的蛋白质的实验结构信息。然而，这些蛋白质中的许多蛋白质都显示出来自计算线程程序的强烈打击，某些结构可以建立同源性，而另一些结构可以从设计良好的力场中预测。该项目的目的是探索剩余的偶极耦合（RDC）约束和顺磁性距离限制的使用，以提高搜索效率和产生的结构的质量。该研究资源将向诸如华盛顿大学的贝克组等计算组提供有关模型蛋白以及糖基转移酶的RDC和距离数据，以便他们可以修改其方法以适应这些类型的NMR数据。目的是开发结构确定的方法，该方法可以与有挑战性的蛋白质一起使用，只能获得有限的结构数据。