Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference.

Abstract

Functionally relevant conformational states of intrinsically disordered proteins (IDPs) are typically concealed in a vast space of fast interconverting structures. Here we present a novel methodology, NMR-based paramagnetic relaxation interference (PRI), that allows for direct observation of concerted motions and cooperatively folded sub-states in IDPs. The proposed NMR technique is based on the exploitation of cross correlated electron-nuclear dipolar relaxation interferences in doubly spin-labeled proteins and probes the transient spatial encounter of electron-nucleus spin pairs.

DOI: 10.1039/c5cp04858c

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@article{Kurzbach2016DetectionOC, title={Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference.}, author={Dennis Kurzbach and Agathe Vanas and Andrea Gabriele Flamm and N Tarnoczi and Georg Kontaxis and Nadica Maltar-Strme{\vc}ki and Katharina Widder and Dariush Hinderberger and Robert Konrat}, journal={Physical chemistry chemical physics : PCCP}, year={2016}, volume={18 8}, pages={5753-8} }