Crystallization of proton channel peptides.
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.
Lovejoy
B
B
Molecular Biology Institute, University of California, Los Angeles 90024-1570.
Akerfeldt
K S
KS
DeGrado
W F
WF
Eisenberg
D
D
D000595:Amino Acid Sequence; D003460:Crystallization; D007202:Indicators and Reagents; D007473:Ion Channels; D008051:Lipid Bilayers; D046911:Macromolecular Substances; D008961:Models, Structural; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D010713:Phosphatidylcholines; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction / Q000379:methods
D007202:Indicators and Reagents; D007473:Ion Channels; D008051:Lipid Bilayers; D046911:Macromolecular Substances; D009842:Oligopeptides; D010713:Phosphatidylcholines; C021016:1,2-diphytanoylphosphatidylcholine