Scott A. Robson

This study identifies two distinct conformational equilibria in arrestin-2 that underlie its pre-activation state in solution.

This study uses NMR and MD simulations to analyze conformational entropy changes in GPCRs, showing how dynamic fluctuations influence allosteric signaling and receptor function.

The study shows the ADGRG6/GPR126 Stachel peptide is intrinsically disordered in solution, with limited helical conformations detected by biophysical experiments.

This paper demonstrates how controlling the CSA tensor geometry in 19F-13C NMR probes can suppress transverse relaxation, enabling optimized probes for large biomolecular systems.

This study investigates the structural stability and orientation of the neurotensin receptor 1 H8-Ctail using NMR in detergent and lipid environments, revealing its sensitivity to membrane conditions.