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Issue 8, 2016
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Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference

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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.

Graphical abstract: Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference

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Publication details

The article was received on 15 Aug 2015, accepted on 21 Sep 2015 and first published on 21 Sep 2015


Article type: Paper
DOI: 10.1039/C5CP04858C
Phys. Chem. Chem. Phys., 2016,18, 5753-5758
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    Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference

    D. Kurzbach, A. Vanas, A. G. Flamm, N. Tarnoczi, G. Kontaxis, N. Maltar-Strmečki, K. Widder, D. Hinderberger and R. Konrat, Phys. Chem. Chem. Phys., 2016, 18, 5753
    DOI: 10.1039/C5CP04858C

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