Low-Frequency Dynamics of BSA Complementarily Studied by Raman and Inelastic Neutron Spectroscopy.

The present study focuses on protein motions on the picosecond time scale, generally characterized by the overlapping of vibrational and relaxational dynamics in disordered molecular systems. Recently, it has been demonstrated that a dry protein, bovine serum albumin (BSA), shows a glass-like transition in the temperature range between 240 and 260 K. Here, we present the results of combined low-frequency Raman and inelastic neutron scattering studies of dry BSA under conditions similar to those of this glass-like transition.