Research in the Prestegard laboratory focuses on nuclear magnetic resonance (NMR) methods development and application of those methods to challenging problems involving soluble proteins, membrane proteins, cell-surface carbohydrates, and carbohydrate-protein interactions. Many of these systems are drug targets and understanding the structural and functional consequences of interactions that mimic drug-biomolecule interactions is a key part of drug design.

Nuclear magnetic resonance (NMR) spectroscopy is rapidly becoming a major contributor of structural and dynamic information on biomolecular systems. The Prestegard laboratory is a leader in both the development and application of new NMR methods. Recent developments include the use of residual dipolar couplings (RDCs), a rich source of orientational information, and new NMR/MS strategies for resonance assignment in large glycosylated proteins. The laboratory also hosts major NMR facilities (including a 900 MHz facility) that contribute to our ability to carry out research.