Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference
Literature Information
D. Kurzbach, A. Vanas, A. G. Flamm, N. Tarnoczi, G. Kontaxis, N. Maltar-Strmečki, K. Widder, D. Hinderberger, R. Konrat
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.
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