MODELING PROTEIN STRUCTURE USING SPARSE NMR CONSTRAINTS

University Of Georgia, Athens GA

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Abstract

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, 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.