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,...

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Bibliographic Details
Published in:Protein science 1992-08, Vol.1 (8), p.1073-1077
Main Authors: Lovejoy, Brett, Åkerfeldt, Karin S., Degrado, William F., Eisenberg, David
Format: Article
Language:English
Subjects:
Amino Acid Sequence
channels
Crystallization
Indicators and Reagents
Ion Channels
ions
Lipid Bilayers
Macromolecular Substances
membrane proteins
Models, Structural
Molecular Sequence Data
Oligopeptides - chemical synthesis
Oligopeptides - chemistry
peptides
Phosphatidylcholines
Protein Structure, Secondary
protons
structure
Structure-Activity Relationship
transport
X-ray diffraction
X-Ray Diffraction - methods
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Summary: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 Å resolution. Earlier it was proposed that the ion‐conducting channels formed by these peptides consist of four peptides associated as a parallel α‐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.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.5560010812