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- W1903442907 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." @default.
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- W1903442907 date "2016-01-01" @default.
- W1903442907 modified "2023-09-26" @default.
- W1903442907 title "Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference" @default.
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- W1903442907 doi "https://doi.org/10.1039/c5cp04858c" @default.
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