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It's a membrane-bound protein, so you could conceivably pack them in pretty tight into some hydrophobic matrix.  I would imagine they'd be pretty stable in a system like that, as proteins are quite happy under those conditions. 

 

The only problem I could see would be how much conformational change the protein needs to go through in order to get the desired effect.  It is my understanding though, that the actual excitation/relaxation is done by the retinal molecule attached to the bacteriorhodopsin.  It's the retinal that is light-sensitive, and it's the protein that facilitates pushing the protons across the cell membrane.  If you're just looking for a color change, and not for proton translocation, you wouldn't need the protein to move that much, if at all.  The retinal/chromophore color change is really all you'd be interested in.  So you'd just need them packed in pretty tight in some crystalline/lattice monolayer.  At least that was my understanding of the article.

 

They've actually been working with these types of phototransducing molecules for a while in bioengineering and nanotech research.  Bacteriorhodopsin was the first membrane protein they got a structure for, way back in the early 70's.  They've done a fair amount of work using them in getting current through membranes, as they are proton pumps, after all.

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Bacteriorhodopsin makes them blood red. these organisms live in the salt evaporation ponds around SF Bay. As the salt concentration goes up, they flourish. Flying into San Francisco or San Jose, you can see blood red ponds below you at certain times of the year. The salt harvested has a red tint to it and has to be washed before being sold.

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