Protein-Based Branched-Photocycle Three-Dimensional Optical Memories.
Abstract
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.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 01, 1997
- Accession Number
- ADA327063
Entities
People
- Robert R. Birge
Organizations
- Syracuse University