Although intrinsically disordered proteins (IDPs) are widespread in Nature and play diverse and important roles in biology, they have so far been little characterized structurally. Auspiciously, intensified efforts using NMR spectroscopy have started to uncover the breadth of their conformational landscape. In particular, polypeptide backbone chemical shifts are emerging as powerful descriptors of local dynamic deviations from the ‘random coil’ (‘rc’) state towards canonical types of secondary structure. These digressions, in turn, can be connected to functional or dysfunctional protein states, for example, in adaptive molecular recognition and protein aggregation.
Here we describe the first inventory of IDP 15N, 1HN, 1Hα, 13CO, 13Cβ , and 13Cα chemical shifts, using data obtained for a set of 14 proteins of unrelated sequence and function.
Sequence-specific random coil chemical shifts of intrinsically disordered proteins. Tamiola K, Acar B, and Mulder FAA. J Am Chem Soc 2010 Dec 29;132(51):18000-3.
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The ncIDP library is available as tabulated ASCII files, and ncIDP program as a web interface running on a server.
The source chemical shift tables are available in the Supporting Information of our 2010 J Am Chem Soc paper (see References).