Tollinger Group, LFU Innsbruck

We study the biophysical properties of proteins by (heteronuclear) nuclear magnetic resonance (NMR) relaxation. We are focussing on kinetic and thermodynamic aspects, which can be critical in biological processes such as enzyme kinetics, allosteric communication and protein folding. Another focus of our group are experimental studies of ligand binding kinetics. We use NMR 15N/13C/1H relaxation dispersion, R1/R2/hetNOE and amide hydrogen exchange experiments, complemented by other biophysicial techniques such as isothermal calorimetry (ITC).