Difference between revisions of "Part:BBa K1642001"

 
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<partinfo>BBa_K1642001 short</partinfo>
 
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Halorhodopsin (HR) proteins are light-driven inward-directed chloride pumps from halobacteria. They are membrane-integral proteins of the rhodopsin superfamily that form a covalent bond with the carotenoid-derived chromophore all-trans retinal. Absorption of a photon with a defined optimal wavelength induces trans-cis isomerization of retinal, which triggers a catalytic photocycle of conformational changes in the protein, resulting in the net import of one chloride per photon into the cytoplasm.[1] And its electrophysiological properties have been characterized in Xenopus laevis oocytes.[2] We use it as our biodesalination driver which confers cyanobacteria the ability to absorb chloride to a significant degree.
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Halorhodopsin (HR) proteins are light-driven inward-directed chloride pumps from halobacteria. They are membrane-integral proteins of the rhodopsin superfamily that form a covalent bond with the carotenoid-derived chromophore all-trans retinal. Absorption of a photon with a defined optimal wavelength induces trans-cis isomerization of retinal, which triggers a catalytic photocycle of conformational changes in the protein, resulting in the net import of one chloride per photon into the cytoplasm(Amezaga, J. M. et al. 2014) . We use it as our biodesalination driver which confers cyanobacteria the ability to absorb chloride to a significant degree. The sequence is codon-optimized so that it would be easier for cyanobacteria to translate the protein.
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His-tag is used to produce anti-His mAb as a first antibody or to purify the protein.
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Latest revision as of 17:59, 18 September 2015

Codon-optimized Halorhodopsin with His-tag

Halorhodopsin (HR) proteins are light-driven inward-directed chloride pumps from halobacteria. They are membrane-integral proteins of the rhodopsin superfamily that form a covalent bond with the carotenoid-derived chromophore all-trans retinal. Absorption of a photon with a defined optimal wavelength induces trans-cis isomerization of retinal, which triggers a catalytic photocycle of conformational changes in the protein, resulting in the net import of one chloride per photon into the cytoplasm(Amezaga, J. M. et al. 2014) . We use it as our biodesalination driver which confers cyanobacteria the ability to absorb chloride to a significant degree. The sequence is codon-optimized so that it would be easier for cyanobacteria to translate the protein.

His-tag is used to produce anti-His mAb as a first antibody or to purify the protein.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 133
    Illegal NgoMIV site found at 292
    Illegal NgoMIV site found at 613
    Illegal AgeI site found at 484
  • 1000
    COMPATIBLE WITH RFC[1000]