James H. Prestegard

TL;DR: The three-dimensional structure of the dimeric transmembrane domain of glycophorin A (GpA) was determined by solution nuclear magnetic resonance spectroscopy of a 40-residue peptide solubilized in aqueous detergent micelles and demonstrates that van der Waals interactions alone can mediate stable and specific associations between trans Membrane helices.

TL;DR: The measurement of dipolar contributions to the splitting of 15N resonances of 1H-15N amide pairs in multidimensional high-field NMR spectra of field-oriented cyanometmyoglobin is reported and implications as an additional source of information for protein structure determination in solution are discussed.

TL;DR: This paper demonstrates that by using singular value decomposition as a method for calculating the order matrices, principal frames and order parameters can be determined efficiently, even when a very limited set of experimental data is available.

TL;DR: Within its relatively short history, nuclear magnetic resonance (NMR) spectroscopy has managed to play an important role in the characterization of biomolecular structure, however, the methods on which most of this characterization has been based, Nuclear Overhauser Effect measurements for short-range distance constraints and scalar couplings measurements for torsional constraints, have limitations.

TL;DR: In this paper, the structure and dynamics of membrane-associated molecules were determined directly from experimental measurements using NMR data, including spin relaxation and magnetic orientation of bilayers, as structural constraints in molecular modeling.