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Documentos Principais

B0184

Sigma-Aldrich

Bacteriorhodopsin from Halobacterium salinarum

native sequence, lyophilized powder

Sinônimo(s):

BR from H. salinarum, Bacterioopsin, Bacteriorhodopsin from Halobacterium halobium

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About This Item

Número CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.56

fonte biológica

Halobacterium salinarium

Formulário

lyophilized powder

técnica(s)

ligand binding assay: suitable
mass spectrometry (MS): suitable

nº de adesão UniProt

temperatura de armazenamento

2-8°C

Informações sobre genes

Halobacterium salinarium ... OE_RS05715(5953595) , VNG_RS05715(144807)

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Descrição geral

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.

Aplicação

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.

Ações bioquímicas/fisiológicas

A transmembrane retinylidine protein that functions as a proton pump driven by light energy in Holobacterium.
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.

Nota de preparo

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.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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Visite a Biblioteca de Documentos

Light-independent phospholipid scramblase activity of bacteriorhodopsin from Halobacterium salinarum
Verchere A, et al.
Scientific reports, 7(1), 9522-9522 (2017)
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)
Bacterioopsin-mediated regulation of bacterioruberin biosynthesis in Halobacterium salinarum
Dummer AM, et al.
Journal of Bacteriology, 193(20), 5658-5667 (2011)
Systematic analysis of protein-detergent complexes applying dynamic light scattering to optimize solutions for crystallization trials
Meyer A, et al.
Acta Crystallographica. Section F, Structural Biology Communications, 71(1), 75-81 (2015)
High production of bacteriorhodopsin from wild type Halobacterium salinarum
Seyedkarimi MS, et al.
Extremophiles : Life Under Extreme Conditions, 19(5), 1021-1028 (2015)

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