Synergistic use of NMR and MD simulations to study the structural heterogeneity of proteins

Nuclear magnetic resonance spectroscopy (NMR) and molecular dynamics (MD) simulations are powerful techniques for the structural characterization of macromolecules. NMR is unique in its ability to provide experimental information at atomic level on the structure as well as on the amplitude and rate of structural fluctuations. MD provides physically sound models and potential mechanisms that connect conformations in time. Nevertheless, none of these techniques allow yet obtaining experimentally validated movies of protein motions at atomic resolution. Instead, it is their complementarity and synergy which offer a unique opportunity toward this end. Here, we overview recent examples that illustrate how much these two techniques benefit from each other, both passively and actively, for the characterization of the structural heterogeneity in proteins.