The use of residual dipolar couplings (RDCs) in the analysis of biomolecular structure and
dynamics has expanded rapidly since its potential as a source of structural information on …

▪ Abstract Recent developments in NMR spectroscopy, which include new experiments that
increase the lifetimes of NMR signals or that precisely define the orientation of internuclear …

▪ Abstract Residual dipolar couplings (RDCs) have recently emerged as a new tool in
nuclear magnetic resonance (NMR) with which to study macromolecular structure and …

The interaction between the amino-terminal transactivation domain (TAD) of p53 and TFIIH
is directly correlated with the ability of p53 to activate both transcription initiation and …

We developed a new program, MSpin‐RDC for the analysis of residual dipolar coupling
data. This software, specially designed for small molecule analysis, can directly read many …

Recent advancements in the utilization of residual dipolar couplings (RDCs) as a means of
structure validation and elucidation have demonstrated the need for, not only a more user …

Determination of relative configuration is frequently a rate-limiting step in the
characterization of small organic molecules. Solution NMR-based nuclear Overhauser effect …

Structural studies of proteins are critical for understanding biological processes at the
molecular level. Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique …

During the last decade anisotropic nuclear magnetic resonance (NMR) parameters
measured in weakly aligned samples have had a profound impact on the structure …

Determination of the accurate three-dimensional structure of large proteins by NMR remains
challenging due to a loss in the density of experimental restraints resulting from the often …