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Results: 1-11 |
Results: 11
Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures
Authors: Balashov, SP Ebrey, TG
Citation: Sp. Balashov et Tg. Ebrey, Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures, PHOTOCHEM P, 73(5), 2001, pp. 453-462
Exploring the function of Tyr83 in bacteriorhodopsin: Features of the Y83Fand Y83N mutants
Authors: Imasheva, ES Lu, M Balashov, SP Ebrey, TG Chen, YM Ablonczy, Z Menick, DR Crouch, RK
Citation: Es. Imasheva et al., Exploring the function of Tyr83 in bacteriorhodopsin: Features of the Y83Fand Y83N mutants, BIOCHEM, 40(44), 2001, pp. 13320-13330
pK(a) of the protonated Schiff base of visual pigments
Authors: Ebrey, TG
Citation: Tg. Ebrey, pK(a) of the protonated Schiff base of visual pigments, METH ENZYM, 315, 2000, pp. 196-207
Evidence for the rate of the final step in the bacteriorhodopsin photocycle being controlled by the proton release group: R134H mutant
Authors: Lu, M Balashov, SP Ebrey, TG Chen, N Chen, YM Menick, DR Crouch, RK
Citation: M. Lu et al., Evidence for the rate of the final step in the bacteriorhodopsin photocycle being controlled by the proton release group: R134H mutant, BIOCHEM, 39(9), 2000, pp. 2325-2331
Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperatures: An FTIR study
Authors: Maeda, A Tomson, FL Gennis, RB Kandori, H Ebrey, TG Balashov, SP
Citation: A. Maeda et al., Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperatures: An FTIR study, BIOCHEM, 39(33), 2000, pp. 10154-10162
Structural biochemistry - Proton pump caught in the act
Authors: Gennis, RB Ebrey, TG
Citation: Rb. Gennis et Tg. Ebrey, Structural biochemistry - Proton pump caught in the act, SCIENCE, 286(5438), 1999, pp. 252-253
How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation
Authors: Nakagawa, M Iwasa, T Kikkawa, S Tsuda, M Ebrey, TG
Citation: M. Nakagawa et al., How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation, P NAS US, 96(11), 1999, pp. 6189-6192
Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp(85) in the Arg(82) his mutant of bacteriorhodopsin
Authors: Imasheva, ES Balashov, SP Ebrey, TG Chen, N Crouch, RK Menick, DR
Citation: Es. Imasheva et al., Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp(85) in the Arg(82) his mutant of bacteriorhodopsin, BIOPHYS J, 77(5), 1999, pp. 2750-2763
The proton release group of bacteriorhodopsin controls the rate of the final step of its photocycle at low pH
Authors: Balashov, SP Lu, M Imasheva, ES Govindjee, R Ebrey, TG Othersen, B Chen, YM Crouch, RK Menick, DR
Citation: Sp. Balashov et al., The proton release group of bacteriorhodopsin controls the rate of the final step of its photocycle at low pH, BIOCHEM, 38(7), 1999, pp. 2026-2039
Chromophore-protein-water interactions in the L intermediate of bacteriorhodopsin: FTIR study of the photoreaction of L at 80 K
Authors: Maeda, A Tomson, FL Gennis, RB Ebrey, TG Balashov, SP
Citation: A. Maeda et al., Chromophore-protein-water interactions in the L intermediate of bacteriorhodopsin: FTIR study of the photoreaction of L at 80 K, BIOCHEM, 38(27), 1999, pp. 8800-8807
Chloride binding regulates the Schiff base pK in gecko P521 cone-type visual pigment
Authors: Yuan, C Kuwata, O Liang, J Misra, S Balashov, SP Ebrey, TG
Citation: C. Yuan et al., Chloride binding regulates the Schiff base pK in gecko P521 cone-type visual pigment, BIOCHEM, 38(14), 1999, pp. 4649-4654
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