NMR contributions to structural dynamics studies of intrinsically disordered proteins

- Cross-correlated NMR spin relaxation probes motional coupling in IDPs.
- NMR and EPR provide insight into the conformational ensemble of IDPs.
- Domain elongation as valuable strategy for decoupling of motional modes in IDPs.
- Conformational substates of IDPs comprise basic protein structural motifs.

Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This article will summarize key advances in basic physical-chemistry and NMR methodology, outline their limitations and envision future R&D directions.

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