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Journal Article | PreJuSER-54323 |
; ; ;
2006
North-Holland Physics Publ.
Amsterdam
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Please use a persistent id in citations: doi:10.1016/j.physb.2006.05.119
Abstract: Results from QENS experiments using a resolution of 93 mu eV on a biological system are reported. The photocycle of the proton pump bacteriorhodopsin (BR) is known to slow down with decreasing temperature and humidity, a behaviour related to the 'dynamic transition'. We have achieved a separation of the pure thermal activation effect involving the plasticizing action of hydration water, from effects due to the variation of the hydration level on the dynamics of purple membrane (PM) with its integral protein BR, and have correlated this with its ability to function. This demonstrates that the biological function of BR requires molecular dynamics in the ps range. (c) 2006 Elsevier B.V. All rights reserved.
Keyword(s): J ; membrane proteins (auto) ; dynamics (auto) ; biological function (auto)
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