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Defining Long-Range Order and Local Disorder in Native r-Synuclein Using Residual Dipolar Couplings

By Pau Bernadó, Carlos W. Bertoncini, Christian Griesinger, Markus Zweckstetter and Martin Blackledge


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

Year: 2008
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