Zusammenfassung
Die Verarbeitung komplexer Muster ist eine Domäne der analogen optischen Datenverarbeitung, bei der die ihr inherente Parallelität zum Tragen kommt. Datendurchsatz und Signal/Rauschverhältnis hängen entscheidend von dem benutzten optischen Verarbeitungsmedium ab. Durch genetische Modifikation des bakteriellen Photochroms Bakteriorhodopsin, welches dem menschlichen Augenpigment Rhodopsin verwandt ist, konnten neue Materialien mit überragender Leistung gewonnen werden.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Literaturverzeichnis
Bräuchte C., N. Hampp, D. Oesterhelt (1991) Optical applications of bacteriorhodopsin and its mutated variants. Adv. Mater. 3:420–428.
Hampp N., C. Bräuchle, D. Oesterhelt (1990a) Bacteriorhodopsin wildtype and variant aspartate-96 → asparagine as reversible holographic media. Biophys. J. 58:83–93.
Hampp N., C. Bräuchle, D. Oesterhelt (1990b) Optical properties of polymeric films of bacteriorhodopsin and its functional variants: new materials for optical information processing. SPIE 1125:2–8.
Hampp N., R. Thoma, D. Zeisel, C. Bräuchle, D. Oesterhelt (1992a) Bacteriorhodopsin variants for holographic pattern recognition. Biomolecular Electronics (im Druck).
Hampp N., A. Popp, C. Bräuchle, D. Oesterhelt (1992b) Diffraction efficiency of bacteriorhodopsin films for holography containing wildtype BRWT and its variants BRD85EN and BRD96N. J. Phys. Chem. 96:4679–4685.
Hampp N., R. Thoma, D. Oesterhelt, C. Bräuchle (1992c) Biological photochrome bacteriorhodopsin and its genetic variant Asp96 → Asn as media for optical pattern recognition. Appl. Opt. 31:1834–1841.
Henderson R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, K. H. Downing (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:899–929.
Kouyama T., K. J. Kinosita, A. Ikegami (1988) Structure and function of bacteriorhodopsin. Adv. Biophys. 24:123–175.
Lee T. C., J. Rebholz, P. Tamura (1979) Dual-axis joint-Fourier-transform correlator. Opt. Lett. 4:121–123.
Mathies R. A., S. W. Lin, J. B. Ames, W. T. Pollard (1991) From femtoseconds to biology: Mechanism of bacteriorhodopsin’s light-driven proton pump. Annu. Rev. Biophys. Biophys. Chem. 20:491–518.
Miller A., D. Oesterhelt (1990) Kinetic optimization of bacteriorhodopsin by aspartic acid 96 as an internal proton donor. Biochim. Biophys. Acta 1020:57–64.
Ni B. F., M. Chang, A. Duschl, J. Lanyi, R. Needleman (1990) An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium. Gene 90:169–172.
Oesterhelt D. (1989) Photosynthetic systems in procaryotes. The retinal proteins of halobacteria and the rection centre of purple bacteria. Biochemistry Intern. 18:673–694.
Oesterhelt D., W. Stoeckenius (1971) Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature (London), New Biol. 233:149–152.
Oesterhelt D., W. Stoeckenius (1974) Isolation of the cell membranes of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:667–678.
Oesterhelt D., C. Bräuchle, N. Hampp (1991) Bacteriorhodopsin: a biological material for information processing. Quart. Rev. Biophys. 24:425–478.
Rajbenbach H., S. Bann, J. P. Huignard (1991) A compact photorefractive joint transform correlator for industrial recognition tasks. Technical digest of optical computing topical meeting, Salt Lake City.
Thoma R., N. Hampp (1992) Real-time holographic correlation of two video signals using bacteriorhodopsin films. Opt. Lett. 17:1158–1160.
Tittor J. (1991) A new view of an old pump: bacteriorhodopsin. Curr. Opin. Struct. Biol. 1:534–538.
Varo G., J. K. Lanyi (1991) Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle. Biochemistry 30:5008–5015.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Hampp, N., Bräuchle, C., Oesterhelt, D. (1993). Gentechnologisch modifizierte Bakteriorhodopsine als neue Materialien für die optische Informationsverarbeitung. In: Hofestädt, R., Krückeberg, F., Lengauer, T. (eds) Informatik in den Biowissenschaften. Informatik aktuell. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78072-1_6
Download citation
DOI: https://doi.org/10.1007/978-3-642-78072-1_6
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-56456-0
Online ISBN: 978-3-642-78072-1
eBook Packages: Springer Book Archive