AssignFit is a computer program developed within the XPLOR-NIH package for the
assignment of dipolar coupling (DC) and chemical shift anisotropy (CSA) restraints derived …

Recent methods of aligning proteins which were developed in order to measure residual
dipolar couplings (RDCs) in solution can also be used for additional applications such as …

The orientation data provided by solid-state NMR can provide a great deal of structural
information about membrane proteins. The quality of the information provided is, however …

In solution NMR spectroscopy the residual dipolar coupling (RDC) is invaluable in improving
both the precision and accuracy of NMR structures during their structural refinement. The …

The two principal components of biological membranes, the lipid bilayer and the proteins
integrated within it, have coevolved for specific functions that mediate the interactions of …

To fully describe the fold space and ultimately the biological function of membrane proteins,
it is necessary to determine the specific interactions of the protein with the membrane. This …

Determination of the three-dimensional (3D) structure of a protein in solution from NMR data
has relied primarily on the measurement of a large number of interproton distances (NOEs) …

An efficient formalism for calculating protein structures from oriented-sample NMR data in
the torsion-angle space is presented. Angular anisotropies of the NMR observables are …

Cross-validation of a solid-state NMR-derived membrane polypeptide structure is
demonstrated. An initial structure has been achieved directly from solid-state NMR derived …

In many cases of protein structure determination by NMR a high‐quality structure is required.
An important contribution to structural precision is stereospecific assignment of magnetically …