B0184
Bacteriorhodopsin from Halobacterium salinarum
native sequence, lyophilized powder
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Synonym(s):
BR from H. salinarum, Bacterioopsin, Bacteriorhodopsin from Halobacterium halobium
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biological source
Halobacterium salinarium
Quality Level
form
lyophilized powder
technique(s)
ligand binding assay: suitable
mass spectrometry (MS): suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
Halobacterium salinarium ... OE_RS05715(5953595) , VNG_RS05715(144807)
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General description
Bacteriorhodopsin (BR) is a covalent complex comprising bacterioopsin protein and retinal cofactor in the equimolar ratio. It corresponds to the molecular weight of 27kDa. BR belongs to the retinylidene class of proteins. It is a seven-membrane helical protein that acts as a photon-driven pump. BR can be used in studies of the folding and kenetics of β-helical proteins.
Bacteriorhodopsin is the prototypical "seven-helix" transmembrane protein (with seven α-helical domains), whose study led to advances in understanding G protein-coupled receptors (GPCRs). In Halobacteria, it acts as a light-harvesting protein, producing a proton gradient across the cell wall that is then used to drive biosynthetic processes.
Application
Bacteriorhodopsin from Halobacterium salinarum has been used:
- in generation of droplet lipid bilayer
- as a standard in quadrupole time-of-flight (QTOF) mass spectroscopy (MS)
- in the generation of protein-detergent complex and micelles for dynamic light scattering studies
Bacteriorhodopsin is of interest in the development of artificial retinas, optical associative processors, and three-dimensional memory storage devices.
Biochem/physiol Actions
Bacteriorhodopsin (BR) from Halobacterium salinarum acts as a proton-driven pump. BR can be used in studies of the folding and kinetics of α-helical proteins. It is thermally stable and exhibits high photoelectric and photochemical efficiency. BR exists as trimer in a hexagonal lattice. Its photocycle intermediates are exploited in bioelectronics majorly in photoelectric and photochemical applications.
A transmembrane retinylidine protein that functions as a proton pump driven by light energy in Holobacterium.
Preparation Note
Aqueous suspensions may be sonicated to achieve the desired homogeneity and may be stored for a short time at a temperature of 2-8 °C or at a temperature of -20 °C without time limitation.
Wild-type bacteriorhodopsin is isolated from Halobacterium salinarum strain S9 as purple membranes.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Protein secondary structure signatures from energy loss spectra recorded in the electron microscope.
Katia March et al.
Journal of microscopy, 282(3), 215-223 (2020-12-12)
Infrared spectroscopy is a powerful technique for characterising protein structure. It is now possible to record energy losses corresponding to the infrared region in the electron microscope and to avoid damage by positioning the probe in the region adjacent to
Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding
Curnow P and Booth PJ
Proceedings of the National Academy of Sciences of the USA, 104(48), 18970-18975 (2007)
Alice Dimonte et al.
Biomacromolecules, 13(11), 3503-3509 (2012-10-11)
Molecular nanoelectronics is attracting much attention, because of the possibility to add functionalities to silicon-based electronics by means of intrinsically nanoscale biological or organic materials. The contact point between active molecules and electrodes must present, besides nanoscale size, a very
High production of bacteriorhodopsin from wild type Halobacterium salinarum
Seyedkarimi MS, et al.
Extremophiles : Life Under Extreme Conditions, 19(5), 1021-1028 (2015)
Best practices and benchmarks for intact protein analysis for top-down mass spectrometry
Donnelly DP, et al,
Nature Methods, 16(7), 587-594 (2019)
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