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. 1993 Dec;65(6):2455-60.
doi: 10.1016/S0006-3495(93)81293-1.

The pore dimensions of gramicidin A

O S Smart  1 , J M Goodfellow, B A Wallace
Affiliations

The pore dimensions of gramicidin A

O S Smart et al. Biophys J. 1993 Dec.

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.

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