Cation-binding location and hydrogen-exchange sites for gramicidin in SDS micelles using NOESY NMR
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. (C) 1996 Academic Press, Inc.
- Journal of Magnetic Resonance Series B
- Start Page
- 1096-0856; 1064-1866