Difference between revisions of "Part:BBa K2229450"

Line 3: Line 3:
 
<partinfo>BBa_K2229450 short</partinfo>
 
<partinfo>BBa_K2229450 short</partinfo>
  
Proteorhodopsin (PR) is a retinal-binding membrane protein commonly known for its function as a light-driven proton pump. This transmembrane protein contains two lysine residue sites - 57 lysine and 59 lysine - that serve as critical citrate-binding sites. The positively charged Lysine residues interact with the negatively charged carboxylate groups, thus inducing a conformational change to the primary structure of PR.  
+
Proteorhodopsin (PR) is a membrane protein of the retinal group commonly known for its function as a light-driven proton pump. This transmembrane protein contains two lysine residue sites - 57 lysine and 59 lysine - that serve as critical citrate-binding sites. The positively charged Lysine residues interact with the negatively charged carboxylate groups, thus inducing a conformational change to the primary structure of PR.  
  
  

Revision as of 07:01, 4 October 2017


Proteorhodopsin (PR) Membrane Receptor

Proteorhodopsin (PR) is a membrane protein of the retinal group commonly known for its function as a light-driven proton pump. This transmembrane protein contains two lysine residue sites - 57 lysine and 59 lysine - that serve as critical citrate-binding sites. The positively charged Lysine residues interact with the negatively charged carboxylate groups, thus inducing a conformational change to the primary structure of PR.


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
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]