Structural fluctuation of proteins revealed by terahertz time-domain spectroscopy

Issue title: From Molecule to Tissue: XIII European Conference on the Spectroscopy of Biological Molecules, Palermo, Italy, August 28–September 2, 2009, Part 1 of 2

Article type: Research Article

Authors: Kambara, Ohki | Tominaga, Keisuke

Affiliations: Molecular Photoscience Research Center, Kobe University, Nada, Kobe, Japan

Note: [] Corresponding author: Ohki Kambara, Molecular Photoscience Research Center, Kobe University, Nada, Kobe 657-8501, Japan. Tel./Fax: +81 78 803 5684; E-mail: [email protected].

Abstract: We have measured spectra of the absorption coefficient and refractive index of hen egg white lysozyme in the wavenumber region from 7 cm−1 to 50 cm−1 by terahertz (THz) time-domain spectroscopy. From comparison with the results of the inelastic neutron scattering experiment it is concluded that analysis of the THz spectra provides information on the vibrational density of states. We studied temperature dependence of the THz spectra as well as hydration effect on them to discuss structural fluctuation of the protein. We observed dynamical transition at around 210 K for lysozyme.

Keywords: Terahertz time-domain spectroscopy, protein, dynamical transition

DOI: 10.3233/SPE-2010-0422

Journal: Spectroscopy, vol. 24, no. 1-2, pp. 149-152, 2010