Synergy between protein fold predictions and 19F NMR

Nuclear magnetic resonance (NMR) spectroscopy is a versatile tool for probing structure, dynamics, folding, and interactions at atomic resolution. While naturally occurring magnetically active isotopes, such as 1H, 13C, or 15N, are most commonly used in biomolecular NMR, 19F is a very attractive and sensitive alternative nucleus, which offers rich information on biomolecules in solution and in the solid state. This presentation will summarize the unique benefits of 19F NMR spectroscopy for the study of biomolecular systems both in vitro and in the cell. I will also report on a recent study in which computational protein fold predictions are assessed experimentally by fluorine NMR methodology.