Reformation of crystalline purple membrane from purified bacteriorhodopsin fragments.
نویسندگان
چکیده
منابع مشابه
The effect of lipid environment in purple membrane on bacteriorhodopsin.
The decay rate of the Bacteriorhodopsin (BR) photocycle intermediate M412 and proton, the proton pump efficiency (H+/M412), the ratios of M412 to other intermediates and the rotational correlation time (tauc) in purple membrane (PM) fragments treated by the zwitterionic detergent 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS) with different concentrations were studied. The r...
متن کاملBacteriorhodopsin precursor. Characterization and its integration into the purple membrane.
Halobacterium halobium spheroplasts synthesize and accumulate a bacteriorhodopsin precursor. By labeling of the precursor with [35S]Met and [3H]Leu followed by Edman degradation, we have confirmed the previous conclusion from the DNA sequencing that the precursor contains 13 additional amino acids at the NH2 terminus of bacteriorhodopsin. Although not processed in the spheroplasts, it integrate...
متن کاملSpin-dependent electron transmission through bacteriorhodopsin embedded in purple membrane.
Spin-dependent photoelectron transmission and spin-dependent electrochemical studies were conducted on purple membrane containing bacteriorhodopsin (bR) deposited on gold, aluminum/aluminum-oxide, and nickel substrates. The result indicates spin selectivity in electron transmission through the membrane. Although the chiral bR occupies only about 10% of the volume of the membrane, the spin polar...
متن کاملRefolding of bacteriorhodopsin from expressed polypeptide fragments.
Bacteriorhodopsin is a heptahelical membrane protein that can be refolded to the native state following denaturation. To analyze the in vitro folding process with independent structural domains, eight fragments comprising two (AB, FG), three (AC, EG), four (AD, DG) or five (AE, CG) of the transmembrane segments were produced by expression in Escherichia coli. The polypeptides were purified to h...
متن کاملMolecular orientation of bacteriorhodopsin within the purple membrane of Halobacterium halobium.
The direction of orientation of the protein bacteriorhodopsin within the purple membrane of Halobacterium halobium has been determined by selected-area electron diffraction of membranes preferentially oriented by adsorption to polylysine. Purple membrane is known to adsorb preferentially to polylysine by its cytoplasmic surface at neutral pH and by its extracellular surface at low pH. To mainta...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 1986
ISSN: 0261-4189
DOI: 10.1002/j.1460-2075.1986.tb04603.x