Structure-function studies on bacteriorhodopsin. V. Effects of amino acid substitutions in the putative helix F.

This publication has 31 references indexed in Scilit:

• Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts regenerated with deuterated tyrosine
  Biochemistry, 1986
• Lac permease of Escherichia: histidine-322 and glutamic acid-325 may be components of a charge-relay system
  Biochemistry, 1986
• An opsin gene expressed in only one photoreceptor cell type of the Drosophila eye
  Cell, 1986
• EFFECTS OF SITE-SPECIFIC AMINO ACID MODIFICATION ON PROTEIN INTERACTIONS AND BIOLOGICAL FUNCTION
  Annual Review of Biochemistry, 1985
• Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation of static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane
  Biochemistry, 1985
• An Asp—Asn substitution in the proteolipid subnit of the ATP‐synthase from Escherichia coli leads to a non‐functional proton channel
  FEBS Letters, 1982
• A proton motive force transducer and its role in proton pumps, proton engines, tobacco mosaic virus assembly and hemoglobin allosterism
  Journal of Theoretical Biology, 1982
• Infrared Spectrum of the Purple Membrane: Clue to a Proton Conduction Mechanism?
  Science, 1982
• An external point-charge model for bacteriorhodopsin to account for its purple color
  Journal of the American Chemical Society, 1980
• A model for proton translocation in biomembranes based on keto-enol shifts in hydrogen bonded peptide groups
  The Journal of Membrane Biology, 1979