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

Mikio Kataoka | Zendy; Hironari Kamikubo | Zendy; Hiroshi Nakagawa | Zendy; Stewart F. Parker | Zendy; Jeremy C. Smith | Zendy

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

Author(s) -

Mikio Kataoka,

Hironari Kamikubo,

Hiroshi Nakagawa,

Stewart F. Parker,

Jeremy C. Smith

Publication year - 2003

Publication title -

journal of spectroscopy

Language(s) - English

Resource type - Journals

eISSN - 2314-4920

pISSN - 2314-4939

DOI - 10.1155/2003/907042

Subject(s) - inelastic neutron scattering , inelastic scattering , protein dynamics , neutron spectroscopy , spectral line , dynamics (music) , chemistry , neutron , neutron scattering , spectroscopy , resolution (logic) , physics , atomic physics , protein structure , crystallography , scattering , nuclear magnetic resonance , nuclear physics , optics , quantum mechanics , astronomy , artificial intelligence , computer science , acoustics

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.

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