Correction: F multiple-quantum coherence NMR spectroscopy for probing protein-ligand interactions.

[This corrects the article DOI: 10.1039/C8RA09296F.].

F multiple-quantum coherence NMR spectroscopy for probing protein-ligand interactions.

A new F NMR method is presented which can be used to detect weak protein binding of small molecules with up to mM affinity. The method capitalizes on the synthetic availability of unique SF containing compounds and the generation of five-quantum coherences (5QC). Given the high sensitivity of 5QC relaxation to exchange events ( reversible protein binding) fragments which bind to the target with weak affinity can be identified.

Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference.

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.