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We have applied inelastic neutron scattering (INS) to the understanding of protein dynamics. INS spectrum of staphy- lococcal 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.

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