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Environmental effects on the protonation states of active site residues in bacteriorhodopsin

Published in: Biophysical Journal

Date of publication: May 1, 1994

Language: English

Bibliographic databases:

Cites articles 30

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Title

Authors

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The interpretation of protein structures: estimation of static accessibility,The interpretation of protein structures: Estimation of static accessibility
August 1, 1974

Energy functions for peptides and proteins. I. Derivation of a consistent force field including the hydrogen bond from amide crystals
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Acid-base equilibrium of the Schiff base in bacteriorhodopsin
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The effect of protonation and electrical interactions on the stereochemistry of retinal schiff bases
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Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation by static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane
November 1, 1988

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
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Crystal structure of rat intestinal fatty-acid-binding protein. Refinement and analysis of the Escherichia coli-derived protein with bound palmitate
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Treatment of electrostatic effects in macromolecular modeling
July 1, 1989

Role of aspartate-96 in proton translocation by bacteriorhodopsin.
June 20, 1990

Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
November 1990

pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model
January 1, 1990

Electrostatic interactions in macromolecules: theory and applications
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 base
July 1, 1990

Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?
July 1, 1991

Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides
May 1, 1991

Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
January 1, 1991

From femtoseconds to biology: mechanism of bacteriorhodopsin's light-driven proton pump
March 1, 1991

Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: purification to homogeneity, pH dependence of pumping, and electron diffraction
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Electrostatic energy and macromolecular function,Electrostatic Energy and Macromolecular Function
March 1, 1992

Perturbing the polar environment of Asp102 in trypsin: consequences of replacing conserved Ser214
April 1, 1992

Proton transfer and energy coupling in the bacteriorhodopsin photocycle
June 1, 1992

Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation,Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple&#x2010;to&#x2010;blue transition of bacteriorhodopsin A solid&#x2010;state13C CP&#x2010;MAS NMR investigation
March 1, 1992

Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
October 1, 1993

Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle
July 1, 1993

Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle
March 1, 1993

Molecular dynamics study of the proton pump cycle of bacteriorhodopsin
March 1, 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 change
March 1, 1993

On the calculation of pKas in proteins
March 1, 1993

Multiple-site titration and molecular modeling: two rapid methods for computing energies and forces for ionizable groups in proteins

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