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Perspective: the essential role of NMR in the discovery and characterization of intrinsically disordered proteins

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Abstract

The 2019 ISMAR Prize recognized NMR studies of disordered proteins. Here we provide a highly personal perspective on the discovery of intrinsically disordered proteins and the development and application of NMR methods to characterize their conformational ensembles, dynamics, and interactions.

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Fig. 1

b, c reproduced with permission from references (Kriwacki et al. 1996; Radhakrishnan et al. 1997)

Fig. 2

Figure adapted from reference (Dyson and Wright 2005) with permission

Fig. 3
Fig. 4

Adapted from reference (Berlow et al. 2017), with permission

Fig. 5

Reproduced from reference (Berlow et al. 2017), with permission

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Acknowledgements

We thank the many members of the Wright and Dyson laboratories, past and present, who have made essential contributions to the IDP work. Sadly, only a few examples of their contributions could be highlighted here. Our work on disordered proteins has been supported by the National Institutes of Health for over 30 years, through grants AI19499 and CA27489 (on anti-peptide antibodies), GM38794 (on peptides), NS14069 and AG21601 (on prions), DK34909 (on protein folding), GM57374 (on peptide NMR), CA96865 (on CBP), CA229652 (on HIF-1α/CITED2 competition), GM113251 (on chaperone interactions), GM56879 and GM075995 (on protein dynamics and p53), and CA214054 (on CREB). We also thank the Skaggs Institute for Chemical Biology for long-term support of our work.

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  1. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA

    H. Jane Dyson & Peter E. Wright

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  1. H. Jane Dyson
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Dyson, H.J., Wright, P.E. Perspective: the essential role of NMR in the discovery and characterization of intrinsically disordered proteins. J Biomol NMR 73, 651–659 (2019). https://doi.org/10.1007/s10858-019-00280-2

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