Abstract

Bacteriorhodopsin (bR) is a reversible photochromic protein that can be used as a holographic medium. The dichroic absorption of the bR molecule is polarization dependent, thereby allowing for the recording of polarization holograms. The properties of polarization holograms can be used to multiplex two independent images in a single bR film. A new technique and associated polarization-multiplexing scheme are demonstrated that allow for simultaneous readout of two orthogonally polarized images while achieving a high normalized diffraction efficiency for each of the individual images.

© 2004 Optical Society of America

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