Cation-Binding Location and Hydrogen-Exchange Sites for Gramicidin in SDS Micelles Using NOESY NMR

Abstract

The site of monovalent cation binding and sites of hydrogen exchange between amide protons and water molecules in the gramicidin A and Phe-1 gramicidin A channels incorporated into SDS micelles have been determined using a NOESY NMR technique. The cation-binding pocket was found to involve residues 10–15 of the peptide.