Myriad biological processes proceed through states that defy characterization by
conventional atomic-resolution structural biological methods. The invisibility of these …

While traditional 1H, 13C, and 15N (HCN) solution state NMR protocols provide a wealth of
data on protein structure and dynamics, 19F NMR provides a unique perspective of …

Paramagnetic metal ions offer outstanding opportunities for protein studies by nuclear
magnetic resonance (NMR) spectroscopy. The paramagnetic effects manifested in the NMR …

NMR spectroscopy is a key method for studying the structure and dynamics of (large)
multidomain proteins and complexes in solution. It plays a unique role in integrated …

Protein-protein interactions and the complexes thus formed are critical elements in a wide
variety of cellular events that require an atomic-level description to understand them in …

Molecules containing unpaired electrons affect the magnetic properties of nuclei in their
vicinity, which is observable in Nuclear Magnetic Resonance (NMR) spectra. As these …

Solvent paramagnetic relaxation enhancement (sPRE) is a versatile nuclear magnetic
resonance (NMR)-based method that allows characterization of the structure and dynamics …

Protein–RNA interactions play essential roles in gene regulation and RNA metabolism.
While high-resolution structures have revealed principles of RNA recognition by individual …

Solvent paramagnetic relaxation enhancement (sPRE) arising from nitroxide-based
cosolutes has recently been used to provide an atomic view of cosolute-induced protein …

Human thymidylate synthase (hTS) is essential for DNA replication and therefore a
therapeutic target for cancer. Effective targeting requires knowledge of the mechanism (s) of …