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Volume 17, Issue 2-3, Pages 529-535

Neutron Inelastic Scattering as a High-Resolution Vibrational Spectroscopy: New Tool for the Study of Protein Dynamics

Mikio Kataoka,1 Hironari Kamikubo,1 Hiroshi Nakagawa,1 Stewart F. Parker,2 and Jeremy C. Smith3

1Graduate School of Materials Science, Nara Institute of Science and Technology (NAIST), Nara 630-0192, Japan
2ISIS Facility, Rutherford Appleton Laboratory, Chilton, Didcot, OX11 0QX, UK
3Interdisciplinary Center for Scientific Computing, University of Heidelberg, INF 368, 69120 Heidelberg, Germany

Copyright © 2003 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.