Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy

Bioinformatic analyses of diverse proteomes predict that intrinsically disordered proteins (IDP) are prevalent throughout living organisms, with particular abundance in eukaryotic proteomes where they play crucial roles in many biochemical processes, including signal transfer, regulation, transcription, and replication and in many human pathologies. The development of experimental and analytical techniques to study IDPs has evolved in parallel over recent years, and one presents a general overview of recent progress in the interpretation of solution-state experimental data, in particular from NMR, to describe the free-energy landscape explored by IDPs. Each NMR resonance reports on an ensemble average over all equivalent nuclei present in the sample and on an average over all conformations that interconvert on rates faster than the so-called chemical shift time scale.