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. 1995 Jun;68(6):2519–2523. doi: 10.1016/S0006-3495(95)80434-0

Dynamics of hydrogen atoms in superoxide dismutase by quasielastic neutron scattering.

C Andreani 1, A Filabozzi 1, F Menzinger 1, A Desideri 1, A Deriu 1, D Di Cola 1
PMCID: PMC1282161  PMID: 7647254

Abstract

The low energy dynamic of the enzyme Cu,Zn superoxide dismutase have been investigated by means of quasielastic neutron scattering in the temperature range 4-320 K. Below 200 K the scattering is purely elastic, while above this temperature a pronounced decrease in the elastic intensity is observed, together with the onset of a small quasielastic component. This behavior is similar to that previously observed in other more flexible globular proteins, and can be attributed to transitions between slightly different conformational substates of the protein tertiary structure. The presence of only a small quasielastic component, whose intensity is < or = 25% of the total spectrum, is related to the high structural rigidity of this protein.

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Selected References

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