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L J Stern

Showing results (41-50 of 63) with videos related to

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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.
Proceedings of the National Academy of Sciences of the United States of America|October 19, 2001
The kinetic basis of peptide exchange catalysis by HLA-DMJ A Zarutskie, R Busch, Z Zavala-Ruiz, et al.
Biochemistry|June 26, 1990
Vibrational spectroscopy of bacteriorhodopsin mutants: evidence for the interaction of proline-186 with the retinylidene chromophoreK J Rothschild, Y W He, T Mogi, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 28, 1999
Extracellular antigen processing and presentation by immature dendritic cellsL Santambrogio, A K Sato, G J Carven, et al.
Biophysical Journal|July 1, 1991
Effects of individual genetic substitutions of arginine residues on the deprotonation and reprotonation kinetics of the Schiff base during the bacteriorhodopsin photocycleG C Lin, M A el-Sayed, T Marti, et al.
Photochemistry and Photobiology|June 1, 1993
Effects of mutagenetic substitution of prolines on the rate of deprotonation and reprotonation of the Schiff base during the photocycle of bacteriorhodopsinY N Zhang, M A el-Sayed, L J Stern, et al.
Nature Structural Biology|February 1, 1995
Intermediates in the folding of the membrane protein bacteriorhodopsinP J Booth, S L Flitsch, L J Stern, et al.
Biochemistry|August 22, 1989
Vibrational spectroscopy of bacteriorhodopsin mutants: chromophore isomerization perturbs tryptophan-86K J Rothschild, D Gray, T Mogi, et al.
Acta Crystallographica. Section D, Biological Crystallography|November 1, 1995
Human class II MHC molecule HLA-DR1: X-ray structure determined from three crystal formsJ H Brown, T S Jardetzky, L J Stern, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1990
Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff baseH Otto, T Marti, M Holz, et al.
Pageof 7

Showing results (41-50 of 63) with videos related to

Sort By:
Pageof 7
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.
Proceedings of the National Academy of Sciences of the United States of America|October 19, 2001
The kinetic basis of peptide exchange catalysis by HLA-DMJ A Zarutskie, R Busch, Z Zavala-Ruiz, et al.
Biochemistry|June 26, 1990
Vibrational spectroscopy of bacteriorhodopsin mutants: evidence for the interaction of proline-186 with the retinylidene chromophoreK J Rothschild, Y W He, T Mogi, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 28, 1999
Extracellular antigen processing and presentation by immature dendritic cellsL Santambrogio, A K Sato, G J Carven, et al.
Biophysical Journal|July 1, 1991
Effects of individual genetic substitutions of arginine residues on the deprotonation and reprotonation kinetics of the Schiff base during the bacteriorhodopsin photocycleG C Lin, M A el-Sayed, T Marti, et al.
Photochemistry and Photobiology|June 1, 1993
Effects of mutagenetic substitution of prolines on the rate of deprotonation and reprotonation of the Schiff base during the photocycle of bacteriorhodopsinY N Zhang, M A el-Sayed, L J Stern, et al.
Nature Structural Biology|February 1, 1995
Intermediates in the folding of the membrane protein bacteriorhodopsinP J Booth, S L Flitsch, L J Stern, et al.
Biochemistry|August 22, 1989
Vibrational spectroscopy of bacteriorhodopsin mutants: chromophore isomerization perturbs tryptophan-86K J Rothschild, D Gray, T Mogi, et al.
Acta Crystallographica. Section D, Biological Crystallography|November 1, 1995
Human class II MHC molecule HLA-DR1: X-ray structure determined from three crystal formsJ H Brown, T S Jardetzky, L J Stern, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1990
Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff baseH Otto, T Marti, M Holz, et al.
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