Trp phosphorescence spectroscopy applied to the study of protein structure and dynamics.

In the design of efficient protein catalysts for applications of industrial, environmental and medical interest, several factors must be considered. Among these, priority is given to the stability of biological macromolecules in the conditions of temperature, pressure and medium in which their function is required or are conserved or marketed. For this purpose, the possibility of obtaining structural information on macromolecules in the physical state and in the conditions of interest is indispensable both to understand the structural determinants of their resistance to particular, and normally unfavorable conditions, and to evaluate the effects of site-specific mutations. These conditions are often unsuitable for studies using conventional spectroscopic techniques, such as fluorescence and circular dichroism. The intrinsic phosphorescence of tryptophan is a technique that in recent years has opened up new perspectives in addressing some of the issues mentioned.
We are currently investigating the effects of various perturbations on the structure and stability of proteins (Az, GFP, NGF, p53), both in the native form and in specially constructed mutants.

Patrizia Cioni (Principal investigator)
Mario D'acunto