期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 18, 期 8, 页码 5753-5758出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5cp04858c
关键词
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资金
- Alexander von Humboldt Foundation
- FWF [P26317-B21, W-1221-B03]
- Austrian Science Fund (FWF) [P26317] Funding Source: Austrian Science Fund (FWF)
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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