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Mark S. Braiman

Veröffentlichungen von Mark S. Braiman zu Braiman, Mark S.. ->
weitere Veröffentlichungen von Mark S. Braiman:
Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin (1994)
Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212 (1988)
Modeling Vibrational Spectra of Amino Acid Side Chains in Proteins: The Carbonyl Stretch Frequency of Buried Carboxylic Residues (1995)
Anion-Protein Interactions during Halorhodopsin Pumping: Halide Binding at the Protonated Schiff Base (1994)
Orientation of the bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopy (1986)
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 change (1993)
Vibrational spectroscopy of bacteriorhodopsin mutants: chromophore isomerization perturbs trytophan-86 (1989)
Fourier transform infrared study of the halorhodopsin chloride pump (1988)
Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine-185 protonates and deprotonantes during the photocycle (1988)
Vibrational analysis of the all-trans-retinal chromophore in light-adapted bacteriorhodopsin (1987)
Veröffentlichungen zu Braiman, Mark S..
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1
Braiman, Mark S.. Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin
In: Biochemistry. - Columbus, Ohio : American Chemical Society, ISSN 1520-4995, Vol. 33, No. 7 (1994), p. 1629-1635
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1994
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2
Braiman, Mark S.. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
In: Biochemistry. - Columbus, Ohio : American Chemical Society, ISSN 1520-4995, Vol. 27, No. 23 (1988), p. 8516-8520
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1988
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3
Dioumaev, Andrei K.. Modeling Vibrational Spectra of Amino Acid Side Chains in Proteins: The Carbonyl Stretch Frequency of Buried Carboxylic Residues
In: American Chemical Society: Journal of the American Chemical Society. - Washington, DC : American Chemical Society, ISSN 1520-5126, Vol. 117, No. 42 (1995), p. 10572-10574
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1995
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4
Walter, Timothy J.. Anion-Protein Interactions during Halorhodopsin Pumping: Halide Binding at the Protonated Schiff Base
In: Biochemistry. - Columbus, Ohio : American Chemical Society, ISSN 1520-4995, Vol. 33, No. 7 (1994), p. 1724-1733
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1994
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5
Earnest, Thomas N.. Orientation of the bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopy
In: Biochemistry. - Columbus, Ohio : American Chemical Society, ISSN 1520-4995, Vol. 25, No. 24 (1986), p. 7793-7798
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1986
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6
Cao, Yi. 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 change
In: Biochemistry. - Columbus, Ohio : American Chemical Society, ISSN 1520-4995, Vol. 32, No. 8 (1993), p. 1981-1990
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1993
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7
Rothschild, Kenneth J.. Vibrational spectroscopy of bacteriorhodopsin mutants: chromophore isomerization perturbs trytophan-86
In: Biochemistry. - Columbus, Ohio : American Chemical Society, ISSN 1520-4995, Vol. 28, No. 17 (1989), p. 7052-7059
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1989
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8
Rothschild, Kenneth J.. Fourier transform infrared study of the halorhodopsin chloride pump
In: Biochemistry. - Columbus, Ohio : American Chemical Society, ISSN 1520-4995, Vol. 27, No. 7 (1988), p. 2420-2424
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1988
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9
Braiman, Mark S.., Mogi, Tatsushi., ... Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine-185 protonates and deprotonantes during the photocycle
in: Proteins: Structure, Function, and Genetics, in: Proteins: Structure, Function, and Genetics . - New York, NY : Wiley-Liss, ISSN 0887-3585, ZDB-ID 1475032-6 Vol. 3 (4. 1988), p. 219-229
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1988
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10
Smith, Steven O.. Vibrational analysis of the all-trans-retinal chromophore in light-adapted bacteriorhodopsin
In: American Chemical Society: Journal of the American Chemical Society. - Washington, DC : American Chemical Society, ISSN 1520-5126, Vol. 109, No. 10 (1987), p. 3108-3125
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1987