Protein-Based Branched-Photocycle Three-Dimensional Optical Memories.
Final rept. Jan 93-Jun 96,
SYRACUSE UNIV NY DEPT OF CHEMISTRY
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The promise of new architecture and more cost effective miniaturization has prompted interest in biomolecular optical memories. We examine here the use of the protein bacteriorhodopsin in a branched photocycle three dimensional memory. By using a sequential one photon process, parallel read and write processes can be carried out without disturbing data outside of the irradiated volume. A bench scale prototype was developed and tested. The prototype used active matrix liquid crystal spatial light modulators, a CCD array detector to monitor the paged data and krypton ion lasers to provide the irradiation. A variety of data cuvettes were prepared to test various optical geometries and protein environments. The protein was optimized by using both thermal and chemical modifications, resulting in a live fold improvement in data write efficiency.
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