Fourier transform infrared spectroscopy (FTIR) coupled with High Pressure (HP) techniques is a suitable tool to investigateunfolding/misfolding processes providing useful information on thekinetics of aggregation of proteins. Since HP affects only the volume contribution to the Gibbs free energy, it is able to perturb the structure of proteins in a reversible way . The principle governing pressureeffects is that it tends to shift a system towards the state that occupies the smallest volume, it causes the electrostriction of charged and polar groups, the elimination of packing defects, and the solvation ofhydrophobic groups. Cavities and packing defects are expected to bemajor contributors to volume changes and their presence will make thesystem more susceptible to pressure unfolding/dissociation. Becausehigh pressure allows stabilization of folding intermediates such asmolten-globule conformations, this method provides an uniqueopportunity for their characterization. We present here latestdevelopments in the set up of a high pressure infrared facility for thestudy of protein folding misfolding and aggregations at the SISSI beamline at Elettra.
|Publication status||Published - 2010|