Nuclear magnetic resonance (NMR) spectroscopy is the most powerful physical method available for the study of molecular structure in the solution state, probing interactions between individual atomic nuclei to reveal their spatial relationships and dynamic properties.
Over recent years, the technique has become steadily more sensitive and widely applicable. At LMB, we use NMR spectrometers with field-strengths ranging from 400MHz to 800MHz, and by combining state-of-the-art, multi-dimensional NMR experiments with sample preparation strategies that employ carefully devised labelling patterns of stable isotopes (e.g. 13C, 15N, 2H), we are able to study detailed three-dimensional solution structures and dynamics in many important biological systems.
A particular strength of NMR is its ability to reveal the structural details of specific interactions between biological macromolecules, especially proteins, and their targets in solution; this is often of crucial importance in understanding the underlying basis of function. We have been using NMR to determine structures and interactions in a variety of highly challenging systems, including particularly proteins and complexes involved in the areas of DNA repair, chromatin targeting, nuclear trafficking, mRNA splicing and vesicle trafficking.
