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The pore dimensions of gramicidin A
O S Smart1, J M Goodfellow, B A Wallace
1Department of Crystallography, Birkbeck College, University of London, England.
Biophysical Journal
|December 1, 1993
Abstract:
The ion channel forming peptide gramicidin A adopts a number of distinct conformations in different environments. We have developed a new method to analyze and display the pore dimensions of ion channels. The procedure is applied to two x-ray crystal structures of gramicidin that adopt distinct antiparallel double helical dimer conformations and a nuclear magnetic resonance (NMR) structure for the beta6.3 NH2-terminal to NH2-terminal dimer. The results are discussed with reference to ion conductance properties and dependence of pore dimensions on the environment.