Methods development in the Prestegard lab is closely connected to the demands of our applications. For example, some exciting diffusion edited amide exchange experiments have been developed for the investigation of the energetics and kinetics of protons involved in hydrogen bonds. Hydrogen bonding is important in stabilizing protein structural elements and it is important in protein-carbohydrate recognition, both subjects under study elsewhere in the lab. Neural network based automated assignment programs for multidimensional NMR spectra have been developed, as have statistics based spectral analysis programs. These programs are essential in making NMR based structural analysis less tedious and more precise.

We are always on a quest to extract new types of information from NMR and related experiments. Current projects involve the use of residual dipolar couplings that occur in molecules oriented by very high magnetic fields, and cross-correlation effects that involve chemical shift anisotropies that also become large in high fields. Both topics rely on the design of new experiments and an in depth theoretical analysis of experimental results.