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.
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