Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: a general mechanism for proton release in bacteriorhodopsin
Open Access
- 30 September 1996
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 71 (3), 1165-1171
- https://doi.org/10.1016/s0006-3495(96)79320-7
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsinBiophysical Journal, 1996
- The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin.1995
- On the calculation of pKas in proteinsProteins-Structure Function and Bioinformatics, 1993
- Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbonsProteins-Structure Function and Bioinformatics, 1991
- Redshift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pHBiophysical Journal, 1991
- From Femtoseconds to Biology: Mechanism of Bacteriorhodopsin's Light-Driven Proton PumpAnnual Review of Biophysics, 1991
- Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopyJournal of Molecular Biology, 1990
- Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212Biochemistry, 1988
- The Effect of Protonation and Electrical Interactions on the Stereochemistry of Retinal Schiff BasesBiophysical Journal, 1985
- Energy functions for peptides and proteins. I. Derivation of a consistent force field including the hydrogen bond from amide crystalsJournal of the American Chemical Society, 1974