Neutron inelastic scattering as a high‐resolution vibrational spectroscopy: New tool for the study of protein dynamics

Issue title: First International Conference on Biomedical Spectroscopy: From molecules to men, Cardiff, UK, 7–10 July 2002, Part II

Article type: Research Article

Authors: Kataoka, Mikio^; | Kamikubo, Hironari | Nakagawa, Hiroshi | Parker, Stewart F. | Smith, Jeremy C.

Affiliations: Graduate School of Materials Science, Nara Institute of Science and Technology (NAIST), Nara 630‐0192, Japan | ISIS Facility, Rutherford Appleton Laboratory, Chilton, Didcot, OX11 0QX, UK | Interdisciplinary Center for Scientific Computing, University of Heidelberg, INF 368, 69120 Heidelberg, Germany

Note: [] Corresponding author. Tel.: +81 743 72 6100; Fax: +81 743 72 6109; E‐mail: kataoka@ms.aist‐nara.ac.jp.

Abstract: We have applied inelastic neutron scattering (INS) to the understanding of protein dynamics. INS spectrum of staphylococcal nuclease (SNase) at 25 K in the energy range between 100 and 4000 cm−1 is compared with the result of normal mode calculation. The theoretical spectrum is in general agreement with experiment and is used to assign the peaks. INS spectra show some significant differences for the folded and the unfolded SNase. The intensity distribution of INS spectrum is different from protein to protein reflecting the differences in amino acid composition. INS is unique and effective for the study of protein dynamics, especially for comparison with theory.

Journal: Spectroscopy, vol. 17, no. 2-3, pp. 529-535, 2003