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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References
Habchi, J., Tompa, P., Longhi, S. & Uversky, V.N. Chem. Rev. 114, 6561–6588 (2014).
van der Lee, R. et al. Chem. Rev. 114, 6589–6631 (2014).
Bhowmick, A. et al. J. Am. Chem. Soc. 138, 9730–9742 (2016).
Dyson, H.J. & Wright, P.E. Nat. Rev. Mol. Cell Biol. 6, 197–208 (2005).
Toth-Petroczy, A. et al. Cell 167, 158–170.e12 (2016).
Fenwick, R.B., van den Bedem, H., Fraser, J.S. & Wright, P.E. Proc. Natl. Acad. Sci. USA 111, E445–E454 (2014).
van den Bedem, H. & Fraser, J.S. Nat. Methods 12, 307–318 (2015).
Ward, A.B., Sali, A. & Wilson, I.A. Science 339, 913–915 (2013).
Lindorff-Larsen, K., Best, R.B., Depristo, M.A., Dobson, C.M. & Vendruscolo, M. Nature 433, 128–132 (2005).
Baldwin, A.J. & Kay, L.E. Nat. Chem. Biol. 5, 808–814 (2009).
Cabrita, L.D. et al. Nat. Struct. Mol. Biol. 23, 278–285 (2016).
Jensen, M.R., Ruigrok, R.W. & Blackledge, M. Curr. Opin. Struct. Biol. 23, 426–435 (2013).
Varadi, M. et al. Nucleic Acids Res. 42, D326–D335 (2014).
Wüthrich, K. Angew. Chem. Int. Ed. Engl. 42, 3340–3363 (2003).
Camilloni, C. et al. Proc. Natl. Acad. Sci. USA 111, 10203–10208 (2014).
Cavalli, A., Salvatella, X., Dobson, C.M. & Vendruscolo, M. Proc. Natl. Acad. Sci. USA 104, 9615–9620 (2007).
De Simone, A., Aprile, F.A., Dhulesia, A., Dobson, C.M. & Vendruscolo, M. eLife 4, e02777 (2015).
Shen, Y. et al. Proc. Natl. Acad. Sci. USA 105, 4685–4690 (2008).
Camilloni, C., De Simone, A., Vranken, W.F. & Vendruscolo, M. Biochemistry 51, 2224–2231 (2012).
Theillet, F.-X. et al. Nature 530, 45–50 (2016).
Waudby, C.A. et al. PLoS One 8, e72286 (2013).
Bonomi, M., Camilloni, C., Cavalli, A. & Vendruscolo, M. Sci. Adv. 2, e1501177 (2016).
Sormanni, P., Camilloni, C., Fariselli, P. & Vendruscolo, M. J. Mol. Biol. 427, 982–996 (2015).
Walsh, I. et al. Bioinformatics 31, 201–208 (2015).
Callaway, E. Nature 525, 172–174 (2015).
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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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DOI: https://doi.org/10.1038/nchembio.2331
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