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Biochemistry|May 19, 1992

Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: analysis by Fourier transform infrared spectroscopyA Maeda, J Sasaki, Y Shichida, et al.

Journal of Biochemistry|March 21, 1998

Stability of the C-terminal alpha-helical domain of bacteriorhodopsin that protrudes from the membrane surface, as studied by high-resolution solid-state 13C NMRS Yamaguchi, S Tuzi, T Seki, et al.

Journal of Molecular Biology|July 25, 2000

Coupling photoisomerization of retinal to directional transport in bacteriorhodopsinH Luecke, B Schobert, J P Cartailler, et al.

Biochemistry|November 12, 1996

Hydration of the counterion of the Schiff base in the chloride-transporting mutant of bacteriorhodopsin: FTIR and FT-raman studies of the effects of anion binding when Asp85 is replaced with a neutral residueY S Chon, J Sasaki, H Kandori, et al.

Science (New York, N.Y.)|July 7, 1995

Conversion of bacteriorhodopsin into a chloride ion pumpJ Sasaki, L S Brown, Y S Chon, et al.

Biochimica Et Biophysica Acta|October 10, 1998

Evidence of local conformational fluctuations and changes in bacteriorhodopsin, dependent on lipids, detergents and trimeric structure, as studied by 13C NMRM Tanio, S Tuzi, S Yamaguchi, et al.

Biochemistry|May 6, 1997

Trp86 --> Phe replacement in bacteriorhodopsin affects a water molecule near Asp85 and light adaptationM Hatanaka, R Kashima, H Kandori, 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.

Biophysical Journal|February 27, 1999

Location of a cation-binding site in the loop between helices F and G of bacteriorhodopsin as studied by 13C NMRS Tuzi, S Yamaguchi, M Tanio, et al.

Proceedings of the National Academy of Sciences of the United States of America|February 15, 1993

Effects of genetic replacements of charged and H-bonding residues in the retinal pocket on Ca2+ binding to deionized bacteriorhodopsinY N Zhang, M A el-Sayed, M L Bonet, et al.

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Showing results (61-70 of 81) with videos related to

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Biochemistry|May 19, 1992

Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: analysis by Fourier transform infrared spectroscopyA Maeda, J Sasaki, Y Shichida, et al.

Journal of Biochemistry|March 21, 1998

Stability of the C-terminal alpha-helical domain of bacteriorhodopsin that protrudes from the membrane surface, as studied by high-resolution solid-state 13C NMRS Yamaguchi, S Tuzi, T Seki, et al.

Journal of Molecular Biology|July 25, 2000

Coupling photoisomerization of retinal to directional transport in bacteriorhodopsinH Luecke, B Schobert, J P Cartailler, et al.

Biochemistry|November 12, 1996

Hydration of the counterion of the Schiff base in the chloride-transporting mutant of bacteriorhodopsin: FTIR and FT-raman studies of the effects of anion binding when Asp85 is replaced with a neutral residueY S Chon, J Sasaki, H Kandori, et al.

Science (New York, N.Y.)|July 7, 1995

Conversion of bacteriorhodopsin into a chloride ion pumpJ Sasaki, L S Brown, Y S Chon, et al.

Biochimica Et Biophysica Acta|October 10, 1998

Evidence of local conformational fluctuations and changes in bacteriorhodopsin, dependent on lipids, detergents and trimeric structure, as studied by 13C NMRM Tanio, S Tuzi, S Yamaguchi, et al.

Biochemistry|May 6, 1997

Trp86 --> Phe replacement in bacteriorhodopsin affects a water molecule near Asp85 and light adaptationM Hatanaka, R Kashima, H Kandori, 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.

Biophysical Journal|February 27, 1999

Location of a cation-binding site in the loop between helices F and G of bacteriorhodopsin as studied by 13C NMRS Tuzi, S Yamaguchi, M Tanio, et al.

Proceedings of the National Academy of Sciences of the United States of America|February 15, 1993

Effects of genetic replacements of charged and H-bonding residues in the retinal pocket on Ca2+ binding to deionized bacteriorhodopsinY N Zhang, M A el-Sayed, M L Bonet, et al.

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