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2. Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle. Heberle J, Dencher NA. Proc Natl Acad Sci U S A; 1992 Jul 01; 89(13):5996-6000. PubMed ID: 1497755 [Abstract] [Full Text] [Related]
3. Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane. Nachliel E, Gutman M, Kiryati S, Dencher NA. Proc Natl Acad Sci U S A; 1996 Oct 01; 93(20):10747-52. PubMed ID: 8855251 [Abstract] [Full Text] [Related]
5. Surface charge changes in purple membranes and the photoreaction cycle of bacteriorhodopsin. Carmeli C, Quintanilha AT, Packer L. Proc Natl Acad Sci U S A; 1980 Aug 01; 77(8):4707-11. PubMed ID: 6254038 [Abstract] [Full Text] [Related]
8. Rapid long-range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk. Alexiev U, Mollaaghababa R, Scherrer P, Khorana HG, Heyn MP. Proc Natl Acad Sci U S A; 1995 Jan 17; 92(2):372-6. PubMed ID: 7831293 [Abstract] [Full Text] [Related]
11. Kinetic isotope effects reveal an ice-like and a liquid-phase-type intramolecular proton transfer in bacteriorhodopsin. le Coutre J, Gerwert K. FEBS Lett; 1996 Dec 02; 398(2-3):333-6. PubMed ID: 8977133 [Abstract] [Full Text] [Related]
12. Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle. Cao Y, Brown LS, Sasaki J, Maeda A, Needleman R, Lanyi JK. Biophys J; 1995 Apr 02; 68(4):1518-30. PubMed ID: 7787037 [Abstract] [Full Text] [Related]
13. Electrooptical studies on proton-binding and -release of bacteriorhodopsin. Tsuji K, Hess B. Eur Biophys J; 1990 Apr 02; 18(1):63-9. PubMed ID: 2155114 [Abstract] [Full Text] [Related]
15. Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumping. Kalisky O, Ottolenghi M, Honig B, Korenstein R. Biochemistry; 1981 Feb 03; 20(3):649-55. PubMed ID: 7213600 [Abstract] [Full Text] [Related]
20. Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp85 in the Arg82 his mutant of bacteriorhodopsin. Imasheva ES, Balashov SP, Ebrey TG, Chen N, Crouch RK, Menick DR. Biophys J; 1999 Nov 03; 77(5):2750-63. PubMed ID: 10545374 [Abstract] [Full Text] [Related] Page: [Next] [New Search]