| Literature DB >> 7508762 |
O S Smart1, J M Goodfellow, B A Wallace.
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.Mesh:
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Year: 1993 PMID: 7508762 PMCID: PMC1225986 DOI: 10.1016/S0006-3495(93)81293-1
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033