Rhodopsin and Halobacteria, Complete Papers
Rhodopsin is a protein which is erasable in PVA 1 million times and it can take pictures with up to 5000 lp/mm.
You can buy it ready or you can grow it. If you want to invest only 10 dollars , halobacterium salinarum is sold live in tubes at high school biology supplier.
Lets start from start of the whole process to make your film.
You bought halobacteria - or halobacterium salinarum - and you want to keep it alive and grow it in glass bottles. Below paper describes how to keep live halobacterium alive !
You will extract rhodopsin from halobacterium, prepare film and expose and read it and delete , rewrite it later in series
Some Effects of Light on the Viability
of Rhodopsin-Containing Halobacteria
THOMAS D. BROCK and SANDRA PETERSEN
Department of Bacteriology, University of Wisconsin, 1550 Linden Drive, Madison, Wisconsin 53706, U.S.A.
Abstract. Under starvation conditions, rhodopsin-containing
halobacteria show a light-accelerated death
under aerobic conditions. This is attributed to photooxidative
processes. Under anaerobic conditions, halobacteria
die rapidly in the dark, and light prevents
death. Since it has been shown by others that lightdriven
ATP synthesis can occur under anaerobic
conditions, it is postulated that rhodopsin-mediated
photophosphorylation is of survival value for this
organism in the brines in which it lives, especially
because the solubility of oxygen is low in highly saline
waters and anaerobic conditions can often develop.
Key words." Rhodopsin - Halobacterium - Starvation
- Photooxidation - Saline environments
Biosynthesis of Rhodopsin from Halobacteria
First post was about halobacteria growing.
This paper relates to biosynthesis of rhodopsin from halobacteria.
Biosynthesis of the Purple Membrane of Halobacteria
By Manfred Sumper, Heribert Reitmeier, and Dieter Oesterhelt[*j
Dedicated to Professor Feodor Ljinen on the occasion of his 65th birthday
Halobacteria are extremely specialized organisms. They live exclusively in saturated solutions
of common salt. The cell membrane of these bacteria exhibit insular regions which can be
isolated by membrane fractionation. These regions consist of a lipid matrix containing bateriorhodopsin
molecules in a hexagonal crystalline arrangement. Bacteriorhodopsin is a deep purple
retinal-protein complex (“purple membrane”). The purple membrane functions as a light energy
converter. --How can such a differentiated membrane region arise? In uiuo studies on the
biosynthesis of the purple membrane showed another cell membrane fraction, the so-called
brown membrane, to be a biosynthetic precursor. Bacterioopsin (the retinal-free protein) is
initially incorporated into the brown membrane and can only form the purple membrane
by crystallization in an energy-dependent reaction after prior reaction with retinal. This reaction
is reversible. Removal of the retinal by formation of retinal oxime causes the purple membrane
regions to disappear. Reconstitution of the bacteriorhodopsin by addition of retinal regenerates
the purple membrane.
Making film out of rhodopsin
You bought bacteria,grew it, synthesized it , now its time to make a film with your rhodopsin.
Bacteriorhodopsin oriented in polyvinyl alcohol films as an erasable optical storage medium
Zhongping Chen, Aaron Lewis, Hiroyuki Takei, and Isaiah Nebenzahl
Films of oriented bacteriorhodopsin have been formed in polyvinyl alcohol with excellent optical quality.
Images with high contrast have been impressed and erased on these films. Second-harmonic microscopy has
been used to read the image on a bacteriorhodopsin-polyvinyl alcohol film without erasure. The potential of
these films for molecular information storage and computation is discussed.
Keywords: Erasable optical storage, bacteriorhodopsin, biomolecular electronic devices
Making 3D Optical Storage and knowing rewrite characteristics of RD
You completed the film and want to learn all about writing, erasing, rewriting characteristics of rhodopsin. This paper is a must and in 4 parts.
Final Technical Report
PROTOTYPE PROTEIN-BASED THREEDIMENSIONAL MEMORY