Biomolecules are characterised by their inherent structural dynamics, which are functionally related to their function. Our research focusses on the structural dynamics of proteins in the millisecond to microsecond range. In this time window, local rearrangements of the three-dimensional structure take place, which enable the binding of bioactive compounds (ligands, enzyme substrates, etc.). NMR spectroscopy allows spatially resolved and quantitative observation of these structural dynamics. The combination with other biophysical methods makes the relationship between structural dynamics and binding affinity experimentally accessible.
NMR relaxation dispersion measurements for the characterisation of functional structural dynamics in biocatalysis.