MODELING PROTEIN STRUCTURE USING SPARSE NMR CONSTRAINTS

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。在合成细胞表面低聚糖，例如糖基转移酶中，许多重要的蛋白质的实验结构信息都很难获得。然而，这些蛋白质中的许多都显示出来自计算线程程序的强大命中率，并且一些结构可以被同源建模。该项目的目标是探索使用剩余偶极耦合(RDC)约束和顺磁距离约束来改进由此产生的结构。研究资源将向佐治亚大学生物化学和分子生物学系的计算小组提供模型蛋白质以及糖基转移酶的RDC和距离数据，以便他们可以修改他们的结构预测方法，以适应这些类型的核磁共振数据的纳入。目标是开发结构确定方法，这种方法可以处理具有挑战性的蛋白质，而这些蛋白质只能获得有限数量的结构数据。

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. 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 and some structures can be homology modeled. The goal of this project is to explore the use of residual dipolar coupling (RDC) restraints and paramagnetic distance restraints in improving the structures that result. The Research Resource will be providing RDC and distance data on model proteins, as well as glycosyltransferases, to the computational group in the Biochemistry and Molecular Biology department at the University of Georgia so they can modify their approaches to structure prediction 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.