Neil A. Farrow

TL;DR: Overall, higher order parameters were not found in the peptide-bound form, indicating that on average, picosecond-time-scale disorder is not reduced upon binding peptide, and the relaxation data of the SH2-phosphopeptide complex were fit with fewer exchange terms than the uncomplexed form.

TL;DR: Simulations demonstrate that the method is accurate for a wide range of protein motions and correlation times, and experimental data establish the validity of the methodology.

TL;DR: A heteronuclear correlation experiment is described which permits simultaneous characterization of both 15N longitudinal decay rates and slow conformational exchange rates, enabling the extraction of accurate rate constants.

TL;DR: Two-dimensional NMR 15N relaxation studies have been used to characterize the backbone dynamics and folding transition of the N-terminal SH3 domain of the protein drk (drkN SH3), showing that while the unfolded state has considerably greater dynamic behavior, the overall motional properties are consistent with it having a reasonably compact structure in solution.

TL;DR: Novel deuterium (2H) based nuclear magnetic resonance (NMR) spin relaxation experiments which probe the nanosecond-picosecond time scale dynamics of methyl containing side chain residues have established that certain regions of the PLCC SH2 domain contacting the residues C-terminal to the pTyr have a high degree of mobility in both the free and peptide complexed states.