Crossref journal-article
Elsevier BV
Journal of Molecular Biology (78)
Bibliography

Bashford, D., & Gerwert, K. (1992). Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin. Journal of Molecular Biology, 224(2), 473–486.

Authors 2
  1. Donald Bashford (first)
  2. Klaus Gerwert (additional)
References 38 Referenced 484
  1. 10.1016/0022-2836(88)90016-2 / J. Mol. Biol / Electrostatic effects of charge perturbations introduced by metal oxidation in proteins by Bashford (1988)
  2. 10.1021/bi00496a010 / Biochemistry / pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model by Bashford (1990)
  3. 10.1021/j100176a093 / J. Phys. Chem / Multiple-site titration curves of proteins: an analysis of exact and approximate methods for their calculation by Bashford (1991)
  4. 10.1021/bi00423a002 / Biochemistry / Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212 by Braiman (1988)
  5. 10.1002/jcc.540040211 / J. Comp. Chem / CHARMM: a program for macromolecular energy, minimization, and dynamics calculations by Brooks (1983)
  6. {'key': '10.1016/0022-2836(92)91009-E_BIB6', 'author': 'Brünger', 'year': '1988'} by Brünger (1988)
  7. 10.1002/prot.340040208 / Proteins / Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison by Brünger (1988)
  8. 10.1002/j.1460-2075.1989.tb03556.x / EMBO J / Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump by Butt (1989)
  9. 10.1021/bi00434a033 / Biochemistry / Nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin: counterion effects on the 15N shift anisotropy by de Groot (1989)
  10. 10.1016/0014-5793(79)80552-9 / FEBS Letters / Bacteriorhodopsin monomers pump protons by Dencher (1979)
  11. 10.1016/S0006-3495(81)84889-8 / Biophys. J / On the mechanism of hydrogen-deuterium exchange in bacteriorhodopsin by Doukas (1981)
  12. 10.1021/bi00263a019 / Biochemistry / Acid-base equilibrium of the Schiff base in bacteriorhodopsin by Druckmann (1982)
  13. 10.1021/bi00323a024 / Biochemistry / Light-driven protonation of 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 by Engelhard (1985)
  14. 10.1016/0014-5793(87)81461-8 / FEBS Letters / Only water-exposed carboxyl groups are protonated during the transition to the cation-free bacteriorhodopsin by Gerwert (1987)
  15. {'key': '10.1016/0022-2836(92)91009-E_BIB15', 'first-page': '4943', 'article-title': 'Role of aspartate-96 in proton translocation by bacteriorhodopsin', 'volume': '86', 'author': 'Gerwert', 'year': '1989'} / Role of aspartate-96 in proton translocation by bacteriorhodopsin by Gerwert (1989)
  16. {'key': '10.1016/0022-2836(92)91009-E_BIB16', 'first-page': '9774', 'article-title': 'Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy', 'volume': '87', 'author': 'Gerwert', 'year': '1990'} / Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy by Gerwert (1990)
  17. 10.1038/330084a0 / Nature (London) / Calculation of electrostatic potentials in an enzyme active site by Gilson (1987)
  18. 10.1016/0022-2836(75)90123-0 / J. Mol. Biol / The structure of the purple membrane from Halobacterium halobium: analysis of the X-ray diffraction pattern by Henderson (1975)
  19. 10.1038/257028a0 / Nature (London) / Three-dimensional model of purple membrane obtained by electron microscopy by Henderson (1975)
  20. 10.1016/S0022-2836(05)80271-2 / J. Mol. Biol / Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy by Henderson (1990)
  21. 10.1021/bi00475a022 / Biochemistry / Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin by Herzfeld (1990)
  22. {'key': '10.1016/0022-2836(92)91009-E_BIB22', 'first-page': '2167', 'article-title': 'Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement', 'volume': '86', 'author': 'Holz', 'year': '1989'} / Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement by Holz (1989)
  23. {'key': '10.1016/0022-2836(92)91009-E_BIB23', 'first-page': '5412', 'article-title': 'Stability of “salt bridges” in membrane proteins', 'volume': '81', 'author': 'Honig', 'year': '1984'} / Stability of “salt bridges” in membrane proteins by Honig (1984)
  24. {'key': '10.1016/0022-2836(92)91009-E_BIB24', 'first-page': '2503', 'article-title': 'Photoisomerization, energy storage, and charge separation: a model for light energy transduction in visual pigments and bacteriorhodopsin', 'volume': '76', 'author': 'Honig', 'year': '1979'} / Photoisomerization, energy storage, and charge separation: a model for light energy transduction in visual pigments and bacteriorhodopsin by Honig (1979)
  25. {'key': '10.1016/0022-2836(92)91009-E_BIB25', 'first-page': '4642', 'article-title': 'Experimental evidence for secondary protein-chromophore interactions at the Schiff base linkage in bacteriorhodopsin: molecular mechanism for proton pumping', 'volume': '75', 'author': 'Lewis', 'year': '1978'} / Experimental evidence for secondary protein-chromophore interactions at the Schiff base linkage in bacteriorhodopsin: molecular mechanism for proton pumping by Lewis (1978)
  26. {'key': '10.1016/0022-2836(92)91009-E_BIB26', 'first-page': '1', 'article-title': 'On the ionisation of proteins', 'volume': '15', 'author': 'Linderstrøm-Lang', 'year': '1924', 'journal-title': 'C.r. Lab. Carlsberg'} / C.r. Lab. Carlsberg / On the ionisation of proteins by Linderstrøm-Lang (1924)
  27. 10.1016/0968-0004(89)90044-3 / Trends Biochem. Sci / Two pumps, one principle: light driven ion transport in halobacteria by Oesterhelt (1989)
  28. {'key': '10.1016/0022-2836(92)91009-E_BIB28', 'first-page': '1018', 'article-title': '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', 'volume': '87', 'author': 'Otto', 'year': '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 by Otto (1990)
  29. 10.1007/BF01593790 / Math. Program / Restart procedures for the conjugate gradient method by Powell (1977)
  30. {'key': '10.1016/0022-2836(92)91009-E_BIB30', 'author': 'Press', 'year': '1986'} by Press (1986)
  31. 10.1146/annurev.bb.06.060177.001055 / Annu. Rev. Biophys. Bioeng / Areas, volumes, packing, and protein structure by Richards (1977)
  32. 10.1038/330086a0 / Nature (London) / Prediction of electrostatic effects of engineering of protein charges by Sternberg (1987)
  33. 10.1146/annurev.bi.51.070182.003103 / Annu. Rev. Biochem / Bacteriorhodopsin and related pigments of halobacteria by Stoeckenius (1982)
  34. {'key': '10.1016/0022-2836(92)91009-E_BIB34', 'first-page': '1013', 'article-title': 'Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82→Ala and Asp-85→Glu: the blue form is inactive in proton translocation', 'volume': '87', 'author': 'Subramaniam', 'year': '1990'} / Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82→Ala and Asp-85→Glu: the blue form is inactive in proton translocation by Subramaniam (1990)
  35. 10.1021/ac60215a007 / Anal. Chem / Nuclear magnetic resonance studies of protonation of polyamine and aminocarboxylate compounds in aqueous solution by Sudmeier (1964)
  36. 10.1021/ja01577a001 / J. Amer. Chem. Soc / Theory of protein titration curves. I. General equations for impenetrable spheres by Tanford (1957)
  37. 10.1021/bi00761a029 / Biochemistry / Interpretation of protein titration curves. Application to lysozyme by Tanford (1972)
  38. 10.1016/S0006-3495(85)83933-3 / Biophys. J / The effect of protonation and electrical interactions on the stereochemistry of retinal Schiff bases by Tavan (1985)
Dates
Type When
Created 20 years, 6 months ago (Feb. 10, 2005, 8:06 a.m.)
Deposited 6 years, 6 months ago (Jan. 28, 2019, 4:27 p.m.)
Indexed 2 months, 2 weeks ago (June 5, 2025, 3:44 a.m.)
Issued 33 years, 5 months ago (March 1, 1992)
Published 33 years, 5 months ago (March 1, 1992)
Published Print 33 years, 5 months ago (March 1, 1992)
Funders 0

None

@article{Bashford_1992, title={Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin}, volume={224}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/0022-2836(92)91009-e}, DOI={10.1016/0022-2836(92)91009-e}, number={2}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Bashford, Donald and Gerwert, Klaus}, year={1992}, month=mar, pages={473–486} }