Crystallization of proton channel peptides

Protein Sci. 1992 Aug;1(8):1073-7. doi: 10.1002/pro.5560010812.


Crystals have been grown of two similar peptides that form ion-conducting channels in diphytanoyl phosphatidylcholine bilayers. These crystals were grown by slow evaporation of the organic solvent, 2,2,2-trifluoroethanol. Crystals of one of the peptides have been characterized by X-ray diffraction, and X-ray data have been measured to 2.3 A resolution. Earlier it was proposed that the ion-conducting channels formed by these peptides consist of four peptides associated as a parallel alpha-helical tetramer. On the basis of the space group and unit cell dimensions of the crystals, a packing scheme for the peptide is proposed that is consistent with a tetrameric channel.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Indicators and Reagents
  • Ion Channels*
  • Lipid Bilayers*
  • Macromolecular Substances
  • Models, Structural
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Phosphatidylcholines
  • Protein Structure, Secondary*
  • Structure-Activity Relationship
  • X-Ray Diffraction / methods


  • Indicators and Reagents
  • Ion Channels
  • Lipid Bilayers
  • Macromolecular Substances
  • Oligopeptides
  • Phosphatidylcholines
  • 1,2-diphytanoylphosphatidylcholine