Paramagnetic chemical probes have been used in electron paramagnetic resonance (EPR)
and nuclear magnetic resonance (NMR) spectroscopy for more than four decades. Recent …

Paramagnetic centers in biomolecules, such as specific metal ions that are bound to a
protein, affect the nuclei in their surrounding in various ways. One of these effects is the …

Macromolecular function frequently requires that proteins change conformation into high-
energy states,,–. However, methods for solving the structures of these functionally essential …

The measurement and application of residual dipolar couplings (RDCs) in solution NMR
studies of biological macromolecules has become well established over the past quarter of a …

The presence of an unpaired electron in paramagnetic molecules generates significant
effects in NMR spectra, which can be exploited to provide restraints complementary to those …

In this review, lanthanide chelating tags and their applications to pseudocontact shift NMR
spectroscopy as well as analysis of residual dipolar couplings are covered. A complete …

In‐cell NMR spectroscopy is an effective tool for observing proteins at atomic resolution in
their native cellular environment. However, its utility is limited by its low sensitivity and the …

NMR chemical shift changes can report on the functional dynamics of biomacromolecules in
solution with sizes> 1 MDa. However, their interpretation requires chemical shift …

Ultra-tight binding is usually observed for proteins associating with rigidified molecules.
Previously, we demonstrated that femtomolar binders derived from the Armadillo repeat …

The paramagnetism of f-block ions has been exploited in chiral shift reagents and magnetic
resonance imaging, but these applications tend to focus on 1H NMR shifts as paramagnetic …