M S Braiman - JoVE Visualize

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Biophysical Journal|February 27, 2001

Halide dependence of the halorhodopsin photocycle as measured by time-resolved infrared spectraM S Hutson, S V Shilov, R Krebs, et al.

The Journal of Biological Chemistry|July 5, 1987

Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coliM S Braiman, L J Stern, B H Chao, et al.

Biochemistry|December 2, 1986

Orientation of the bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopyT N Earnest, P Roepe, M S Braiman, et al.

The Journal of Biological Chemistry|October 5, 1990

Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence for the interaction of aspartic acid 212 with tyrosine 185 and possible role in the proton pump mechanismK J Rothschild, M S Braiman, Y W He, et al.

Biochemistry|October 29, 2000

Evidence for a perturbation of arginine-82 in the bacteriorhodopsin photocycle from time-resolved infrared spectraM S Hutson, U Alexiev, S V Shilov, et al.

Biochemistry|April 5, 1988

Fourier transform infrared study of the halorhodopsin chloride pumpK J Rothschild, O Bousché, M S Braiman, et al.

FEBS Letters|July 3, 1989

Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocketK J Rothschild, M S Braiman, T Mogi, et al.

Experimental Eye Research|June 17, 1998

Soluble expression in E. coli of a functional interphotoreceptor retinoid-binding protein module fused to thioredoxin: correlation of vitamin A binding regions with conserved domains of C-terminal processing proteasesC A Baer, J D Retief, E Van Niel, et al.

Biochemistry|November 15, 1988

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212M S Braiman, T Mogi, T Marti, et al.

Biochemistry|March 2, 1993

Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational changeY Cao, G Váró, A L Klinger, et al.

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Showing results (11-20 of 26) with videos related to

Sort By:

Pageof 3

Biophysical Journal|February 27, 2001

Halide dependence of the halorhodopsin photocycle as measured by time-resolved infrared spectraM S Hutson, S V Shilov, R Krebs, et al.

The Journal of Biological Chemistry|July 5, 1987

Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coliM S Braiman, L J Stern, B H Chao, et al.

Biochemistry|December 2, 1986

Orientation of the bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopyT N Earnest, P Roepe, M S Braiman, et al.

The Journal of Biological Chemistry|October 5, 1990

Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence for the interaction of aspartic acid 212 with tyrosine 185 and possible role in the proton pump mechanismK J Rothschild, M S Braiman, Y W He, et al.

Biochemistry|October 29, 2000

Evidence for a perturbation of arginine-82 in the bacteriorhodopsin photocycle from time-resolved infrared spectraM S Hutson, U Alexiev, S V Shilov, et al.

Biochemistry|April 5, 1988

Fourier transform infrared study of the halorhodopsin chloride pumpK J Rothschild, O Bousché, M S Braiman, et al.

FEBS Letters|July 3, 1989

Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocketK J Rothschild, M S Braiman, T Mogi, et al.

Experimental Eye Research|June 17, 1998

Soluble expression in E. coli of a functional interphotoreceptor retinoid-binding protein module fused to thioredoxin: correlation of vitamin A binding regions with conserved domains of C-terminal processing proteasesC A Baer, J D Retief, E Van Niel, et al.

Biochemistry|November 15, 1988

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212M S Braiman, T Mogi, T Marti, et al.

Biochemistry|March 2, 1993

Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational changeY Cao, G Váró, A L Klinger, et al.

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