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M Ottolenghi

Showing results (11-20 of 47) with videos related to

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Biophysical Journal|July 1, 1976
On the primary quantum yields in the bacteriorhodopsin photocycleC R Goldschmidt, M Ottolenghi, R Korenstein
Biochemistry|September 19, 1995
pKa of the protonated Schiff base and aspartic 85 in the bacteriorhodopsin binding site is controlled by a specific geometry between the two residuesI Rousso, N Friedman, M Sheves, et al.
Biochemistry|October 18, 1994
Factors affecting the formation of an M-like intermediate in the photocycle of 13-cis-bacteriorhodopsinG Steinberg, M Sheves, S Bressler, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1986
Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analoguesM Sheves, A Albeck, N Friedman, et al.
Biochemistry|February 3, 1981
Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumpingO Kalisky, M Ottolenghi, B Honig, et al.
Biochemistry|April 8, 1997
Interaction between Asp-85 and the proton-releasing group in bacteriorhodopsin. A study of an O-like photocycle intermediateY Gat, N Friedman, M Sheves, et al.
Biophysical Journal|July 1, 1991
Organization and dynamics of pyrene and pyrene lipids in intact lipid bilayers. Photo-induced charge transfer processesY Barenholz, T Cohen, R Korenstein, et al.
Biophysical Journal|July 1, 1977
Electric field effects in bacteriorhodopsinR Shinar, S Druckmann, M Ottolenghi, et al.
Biophysical Journal|July 21, 2001
Specific binding sites for cations in bacteriorhodopsinT Eliash, L Weiner, M Ottolenghi, et al.
The Journal of Biological Chemistry|May 10, 2000
Bacteriorhodpsin experiences light-induced conformational alterations in nonisomerizable C(13)=C(14) pigments. A study with EPRA Aharoni, L Weiner, M Ottolenghi, et al.
Pageof 5

Showing results (11-20 of 47) with videos related to

Sort By:
Pageof 5
Biophysical Journal|July 1, 1976
On the primary quantum yields in the bacteriorhodopsin photocycleC R Goldschmidt, M Ottolenghi, R Korenstein
Biochemistry|September 19, 1995
pKa of the protonated Schiff base and aspartic 85 in the bacteriorhodopsin binding site is controlled by a specific geometry between the two residuesI Rousso, N Friedman, M Sheves, et al.
Biochemistry|October 18, 1994
Factors affecting the formation of an M-like intermediate in the photocycle of 13-cis-bacteriorhodopsinG Steinberg, M Sheves, S Bressler, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1986
Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analoguesM Sheves, A Albeck, N Friedman, et al.
Biochemistry|February 3, 1981
Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumpingO Kalisky, M Ottolenghi, B Honig, et al.
Biochemistry|April 8, 1997
Interaction between Asp-85 and the proton-releasing group in bacteriorhodopsin. A study of an O-like photocycle intermediateY Gat, N Friedman, M Sheves, et al.
Biophysical Journal|July 1, 1991
Organization and dynamics of pyrene and pyrene lipids in intact lipid bilayers. Photo-induced charge transfer processesY Barenholz, T Cohen, R Korenstein, et al.
Biophysical Journal|July 1, 1977
Electric field effects in bacteriorhodopsinR Shinar, S Druckmann, M Ottolenghi, et al.
Biophysical Journal|July 21, 2001
Specific binding sites for cations in bacteriorhodopsinT Eliash, L Weiner, M Ottolenghi, et al.
The Journal of Biological Chemistry|May 10, 2000
Bacteriorhodpsin experiences light-induced conformational alterations in nonisomerizable C(13)=C(14) pigments. A study with EPRA Aharoni, L Weiner, M Ottolenghi, et al.
Pageof 5