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Jaka Kragelj, Dr. Valéry Ozenne, Dr. Martin Blackledge and Dr. Malene Ringkjøbing Jensen Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts ChemPhysChem 14

Version of Record online: 21 JUN 2013 | DOI: 10.1002/cphc.201300387

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Understanding protein disorder: Over the last decade, classical structural biology has experienced a shift towards a more dynamic paradigm with the realization that a protein can be fully functional even in the absence of a stable, folded structure. In this review the recent advances in the determination of conformational propensities of intrinsically disordered proteins at atomic resolution from experimental NMR chemical shifts are presented.

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