Raman spectroscopy: a useful tool to probe protein structural changes

Raman spectroscopy has become a versatile tool in protein science and biotechnology thanks to the improved instrument sensitivity which has increased the signal-to-noise ratio. Thus, this technique can be successfully used for determination of protein secondary structure, identification of metal coordination sites, hydrogen bonding, oxidation state and local environments of selected residues (i.e. Cys, Tyr, Trp), protein-ligand and -DNA interactions, etc. The advantages of this spectroscopic technique are its extreme sensitivity to changes in structure and molecular interaction and its non-destructive nature. In particular, in our lab, Raman spectroscopy has been recently used for obtaining structural information on changes induced by different stimuli: • thermal aggregation: beta-lactoglobulin and bovine serum albumin; • presence of metal ions: metallothioneins; • adsorption of biomedical devices: self-assembling peptides; • damages induced by radical stress: human serum albumin; • thermal or chemical denaturation: lysozime.