Dynamical properties of proteins

The peculiar dynamical properties of proteins arise from their complex nature, which can be well described in terms of a multi-minima energy landscape. In fact, proteins may exist in a very large number of slightly different structures, known as Conformational Substates. At low temperature, each protein molecule is confined in one substate, and the system behaves as a harmonic solid. On the contrary, at high temperature, typically above ~200 K, proteins start to fluctuate among different substates. This phenomenon, known as Protein Dynamical Transition, brings about a steep increase in all dynamical properties of protein, with the onset specific motions which are crucial for their functionality, since they give to protein molecules the flexibility which is necessary to perform their function, whatever it is. These processes can be investigated by means of conventional experimental techniques, such as Infrared Spectroscopy, or by using large facilities as in Neutron Scattering.

Members:
Rita Carrotta
Fabio Librizzi (Principal investigator)