Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins.

Míreanna Comhchosúla

• Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model.
  le: Brown, L S, et al.
  Foilsithe: (1998)
• Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation.
  le: Duñach, M, et al.
  Foilsithe: (1990)
• Decoupling of photo- and proton cycle in the Asp85-->Glu mutant of bacteriorhodopsin.
  le: Heberle, J, et al.
  Foilsithe: (1993)
• Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle.
  le: Brown, L S, et al.
  Foilsithe: (1993)
• Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation.
  le: Subramaniam, S, et al.
  Foilsithe: (1990)