The conformational flexibility inherent to natively unfolded proteins places them beyond the reach of classical structural biology. It is, however, becoming clear that these proteins participate in a vast range of biochemical processes, 1 and that their native plasticity bestows specific functional properties. 2 In contrast to structured proteins, intrinsically unfolded proteins must be described by an ensemble of interconverting conformers. Residual dipolar couplings (RDCs) 3 report on time and ensemble-averaged conformations up to the millisecond time scale 4 and can, therefore, be used to characterize both the structure and dynamics of unfolded proteins. 5 In this study, we present a novel interpretation of RDCs that simultaneously describes long-range structural order and local conformational sampling. This approach is used to describe the structure and dynamics of R-Synuclein (RS), a 140 amino acid protein found in human brain and strongly implicated in the onse
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