منابع مشابه
Unravelling the folding of bacteriorhodopsin.
The folding mechanism of integral membrane proteins has eluded detailed study, largely as a result of the inherent difficulties in folding these proteins in vitro. The seven-transmembrane helical protein bacteriorhodopsin has, however, allowed major advances to be made, not just on the folding of this particular protein, but also on the factors governing folding of transmembrane alpha-helical p...
متن کاملA transposable element from Halobacterium halobium which inactivates the bacteriorhodopsin gene.
We describe the characterization of a transposable element from an archaebacterium. The bacteriorhodopsin genes from the wild-type and two mutant Halobacterium halobium strains have been cloned as BamHI fragments in pBR322. The cloned DNA fragments from the two mutants both contain a 1.1-kilobase-pair insertion sequence (ISH1) near the NH2 terminus of the bacteriorhodopsin coding sequence. ISH1...
متن کاملColor recognition with bacteriorhodopsin.
We have studied opto-electric properties of wild type bacteriorhodopsin and its two artificial variants. We have measured opto-electric responses with respect to wavelength for all three proteins and we describe the use of the proteins for color detection. Opto-electric responses of proteins to set of colored lights were measured and it has been shown that bacteriorhodopsin and its variants can...
متن کاملBacteriorhodopsin optoelectronic synapses.
Synapses are critical components of an artificial neural network. Bacteriorhodopsin thin film can be used to construct compact, finely graded synapses for an optoelectronic neural network, based on its photochromic properties. Measurements show that these photochromic changes are blocked at low temperature. Thermal gating will allow synapses to be written on the film optically and then read wit...
متن کاملProtein conformational changes in the bacteriorhodopsin photocycle.
We report a comprehensive electron crystallographic analysis of conformational changes in the photocycle of wild-type bacteriorhodopsin and in a variety of mutant proteins with kinetic defects in the photocycle. Specific intermediates that accumulate in the late stages of the photocycle of wild-type bacteriorhodopsin, the single mutants D38R, D96N, D96G, T46V, L93A and F219L, and the triple mut...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1981
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.78.11.6744