Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation.

Παρόμοια τεκμήρια

• Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base.
  ανά: Otto, H, κ.ά.
  Έκδοση: (1990)
• Locations of Arg-82, Asp-85, and Asp-96 in helix C of bacteriorhodopsin relative to the aqueous boundaries.
  ανά: Greenhalgh, D A, κ.ά.
  Έκδοση: (1991)
• 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.
  ανά: Subramaniam, S, κ.ά.
  Έκδοση: (1990)
• Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins.
  ανά: Richter, H T, κ.ά.
  Έκδοση: (1996)
• Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle.
  ανά: Brown, L S, κ.ά.
  Έκδοση: (1993)