During the folding process, a protein molecule that is composed of a linear chain of amino acids shapes itself into a complex and unique three-dimensional structure that allows it to perform its specific role in the biology of an organism. Many of such functional roles may involve conformational changes of the folded protein that respond to a variety of physical-chemical stimuli, including temperature, pressure, and reagent molecules. Our research activities are then mainly devoted to understand the folding process of proteins, their molecular motions in the functional folded state and their physical-chemical modulation by external forces and ligands. Either soluble or membrane proteins are investigated, under modulatory effects induced by physical changes in the environment, molecular binding of small ligands and other proteins. More details can be found in Publications.