UV-Excited Resonance Raman Spectra of Heat Denatured Lysozyme and Staphylococcus Epidermidis

The authors have measured the UV resonance Raman spectra of the well-characterized protein lysozyme (which contains both tryptophan and proline) and Staphylococcus epidermidis, both before and after heating at 60°C for 30 min. We have examined the spectra changes due to heating for both lysozyme and the bacteria with a view to relating the effect of conformational changes due to heating to changes in UV resonance Raman excited protein spectra. It is observed that there are substantial spectral changes for lysozyme and S. epidermidis upon heating at 60°C. Even though the changes in the 1340- and 1456-cm-1 modes of lysozyme are the only ones which seem to be explained in terms of previous spectral studies, the other changes are probably related to changes in protein conformation also and suggest that careful studies of the relation between protein structure and the energy and intensity of these modes may be warranted in the future.