Nuclear magnetic resonance spectroscopy is transforming our views of proteins by revealing how their structures and dynamics are closely intertwined to underlie their functions and interactions. Compelling representations of proteins as statistical ensembles are uncovering the presence and biological relevance of conformationally heterogeneous states, thus gradually making it possible to go beyond the dichotomy between order and disorder through more quantitative descriptions that span the continuum between them.
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This work was funded in part by COST ACTION bm1405 NGP-net.
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Sormanni, P., Piovesan, D., Heller, G. et al. Simultaneous quantification of protein order and disorder. Nat Chem Biol 13, 339–342 (2017). https://doi.org/10.1038/nchembio.2331
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