AAAAAA

   
Results: 1-11 |
Results: 11
Ultrafast spectroscopy of the protonated Schiff bases of free and C-13=C-14 locked retinals
Authors: Hou, B Friedman, N Ruhman, S Sheves, M Ottolenghi, M
Citation: B. Hou et al., Ultrafast spectroscopy of the protonated Schiff bases of free and C-13=C-14 locked retinals, J PHYS CH B, 105(29), 2001, pp. 7042-7048
Specific binding sites for cations in bacteriorhodopsin
Authors: Eliash, T Weiner, L Ottolenghi, M Sheves, M
Citation: T. Eliash et al., Specific binding sites for cations in bacteriorhodopsin, BIOPHYS J, 81(2), 2001, pp. 1155-1162
Retinal isomerization in bacteriorhodopsin is controlled by specific chromophore-protein interactions. A study with noncovalent artificial pigments
Authors: Aharoni, A Ottolenghi, M Sheves, M
Citation: A. Aharoni et al., Retinal isomerization in bacteriorhodopsin is controlled by specific chromophore-protein interactions. A study with noncovalent artificial pigments, BIOCHEM, 40(44), 2001, pp. 13310-13319
Nonisomerizable non-retinal chromophores initiate light-induced conformational alterations in bacterioopsin
Authors: Aharoni, A Weiner, L Lewis, A Ottolenghi, M Sheves, M
Citation: A. Aharoni et al., Nonisomerizable non-retinal chromophores initiate light-induced conformational alterations in bacterioopsin, J AM CHEM S, 123(27), 2001, pp. 6612-6616
Bacteriorhodpsin experiences light-induced conformational alterations in nonisomerizable C-13=C-14 pigments - A study with EPR
Authors: Aharoni, A Weiner, L Ottolenghi, M Sheves, M
Citation: A. Aharoni et al., Bacteriorhodpsin experiences light-induced conformational alterations in nonisomerizable C-13=C-14 pigments - A study with EPR, J BIOL CHEM, 275(28), 2000, pp. 21010-21016
On the protein residues that control the yield and kinetics of O-630 in the photocycle of bacteriorhodopsin
Authors: Li, Q Bressler, S Ovrutsky, D Ottolenghi, M Friedman, N Sheves, M
Citation: Q. Li et al., On the protein residues that control the yield and kinetics of O-630 in the photocycle of bacteriorhodopsin, BIOPHYS J, 78(1), 2000, pp. 354-362
Vibrational spectrum of a picosecond intermediate in the artificial BR5.12photoreaction: Picosecond time-resolved CARS of T5.12
Authors: Ujj, L Zhou, YD Sheves, M Ottolenghi, M Ruhman, S Atkinson, GH
Citation: L. Ujj et al., Vibrational spectrum of a picosecond intermediate in the artificial BR5.12photoreaction: Picosecond time-resolved CARS of T5.12, J AM CHEM S, 122(1), 2000, pp. 96-106
On the nature of the primary light-induced events in bacteriorhodopsin: Ultrafast spectroscopy of native and C-13=C-14 locked pigments
Authors: Ye, T Friedman, N Gat, Y Atkinson, GH Sheves, M Ottolenghi, M Ruhman, S
Citation: T. Ye et al., On the nature of the primary light-induced events in bacteriorhodopsin: Ultrafast spectroscopy of native and C-13=C-14 locked pigments, J PHYS CH B, 103(24), 1999, pp. 5122-5130
The titrations of Asp-85 and of the cation binding residues in bacteriorhodopsin are not coupled
Authors: Eliash, T Ottolenghi, M Sheves, M
Citation: T. Eliash et al., The titrations of Asp-85 and of the cation binding residues in bacteriorhodopsin are not coupled, FEBS LETTER, 447(2-3), 1999, pp. 307-310
Resolving the primary dynamics of bacteriorhodopsin, and of a 'C-13=C-14 locked' analog, in the reactive excited state
Authors: Ye, T Gershgoren, E Friedman, N Ottolenghi, M Sheves, M Ruhman, S
Citation: T. Ye et al., Resolving the primary dynamics of bacteriorhodopsin, and of a 'C-13=C-14 locked' analog, in the reactive excited state, CHEM P LETT, 314(5-6), 1999, pp. 429-434
Generation of the O-630 photointermediate of bacteriorhodopsin is controlled by the state of protonation of several protein residues
Authors: Bressler, S Friedman, N Li, Q Ottolenghi, M Saha, C Sheves, M
Citation: S. Bressler et al., Generation of the O-630 photointermediate of bacteriorhodopsin is controlled by the state of protonation of several protein residues, BIOCHEM, 38(7), 1999, pp. 2018-2025
Risultati: 1-11 |