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The pore dimensions of gramicidin A
December 1993
December 1993
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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.