MODELING PROTEIN STRUCTURE USING SPARSE NMR CONSTRAINTS

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。对于许多在细胞表面寡糖合成中起重要作用的蛋白质，例如糖基转移酶，很难获得实验结构信息。然而，这些蛋白质中的许多显示出来自计算线程程序的强烈命中，并且一些结构可以被同源建模。这个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，以改善结构的结果。研究资源将提供RDC和模型蛋白质的距离数据，以及糖基转移酶，在生物化学和分子生物学系计算组在格鲁吉亚大学，使他们可以修改他们的方法来结构预测，以适应这些类型的NMR数据的列入。其目标是开发用于结构测定的方法，该方法可以用于仅可以获得有限数量的结构数据的具有挑战性的蛋白质。

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.