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Updated: Apr 2, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic
D Kurzbach1, A Vanas1, A G Flamm1
1Department for Structural and Computational Biology Max F. Perutz Laboratories, University of Vienna Vienna Biocenter Campus 5, 1030 Vienna, Austria. Robert.Konrat@univie.ac.at.
None:
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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