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Issue 24, 2009
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Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin

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Abstract

Membrane proteins are laterally coupled to the surrounding cell membrane through complex interactions that can modulate their function. Here, we directly observe and quantify the dynamics of functioning bacteriorhodopsin (bR) in its native membrane, a crystalline aggregate of bR trimers. We show that much of a monomer's isomerization energy is mechanically redistributed into the membrane, producing cooperative activity within the trimer while simultaneously generating functionally relevant long-range lateral pressure waves. Our results provide evidence of coordinated short and long-range effects in the cell membrane.

Graphical abstract: Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin

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Publication details

The article was received on 30 Apr 2009, accepted on 08 Sep 2009 and first published on 27 Oct 2009


Article type: Paper
DOI: 10.1039/B908635H
Soft Matter, 2009,5, 4899-4904

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    Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin

    K. Voïtchovsky, S. A. Contera and J. F. Ryan, Soft Matter, 2009, 5, 4899
    DOI: 10.1039/B908635H

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