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Quantification of thermal motions in the purple membrane

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78468

Oesterhelt,  D.
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Lehnert, U., Reat, V., Kessler, B., Oesterhelt, D., & Zaccai, G. (2002). Quantification of thermal motions in the purple membrane. Applied Physics A-Materials Science & Processing, 74(Suppl. S), S1287-S1289.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6DCC-E
Zusammenfassung
Local atomic motions in bacteriorhodopsin (BR), the membrane protein in purple membranes (PMs) of Halobacterium salinarum, were studied by incoherent neutron scattering. The analysed sample consisted of fully deuterated purple membranes with BR- containing H-retinal, H-tryptophan, and H-methionine. These labelled groups are present in the retinal binding pocket and the extracellular part of BR. By using incoherent neutron scattering on two different backscattering instruments at the Institut Laue-Langevin, we. determined the mean-square displacements of small- and large-amplitude motions as a function of temperature for labelled as well as completely hydrogenated PM samples at different hydration states. We showed that the dynamics of the labelled part is more rigid, and influenced by temperature and hydration in a different way, than the membrane globally.