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Thermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering.

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Ferrand, M, Dianoux, A J, Petry, W, Zaccaï, G·1993·Proceedings of the National Academy of Sciences

Abstract

The internal dynamics of bacteriorhodopsin, the light-driven proton pump in the purple membrane of Halobacterium halobium, has been studied by inelastic neutron scattering for various conditions of temperature and hydration. Light activation can take place when the membrane is vibrating harmonically. The ability of the protein to functionally relax and complete the photocycle initiated by the absorption of a photon, however, is strongly correlated with the onset of low-frequency, large-amplitude anharmonic atomic motions in the membrane. For a normally hydrated sample, this occurs at about 230 K, where a dynamical transition from a low-temperature harmonic regime is observed. In moderately dry samples, on the other hand, in which the photocycle is slowed down by several orders of magnitude, no transition is observed and protein motions remain approximately harmonic up to room temperature. These results support the hypothesis, made from previous neutron diffraction studies, that the "softness" of the membrane modulates the function of bacteriorhodopsin by allowing or not allowing large-amplitude motions in the protein.

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Metadata

Authors
Ferrand, M., Dianoux, A. J., Petry, W., & Zaccaï, G.
Venue
Proceedings of the National Academy of Sciences
Published
1993-10-15
Volume
90
Issue
20
Pages
9668-9672
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2052495184
Cited by
389
References
0
FWCI
0.57
Type
journal article
Language
en
Open access
green

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Ferrand, M., Dianoux, A. J., Petry, W., & Zaccaï, G. (1993). Thermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.20.9668

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