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.
Hinton
J F
JF
Department of Chemistry/Biochemistry, University of Arkansas, Fayetteville 72701, USA.
D000595:Amino Acid Sequence; D002412:Cations; D006096:Gramicidin / Q000737:chemistry*; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008969:Molecular Sequence Data; D012967:Sodium Dodecyl Sulfate
D002412:Cations; D008823:Micelles; D006096:Gramicidin; D012967:Sodium Dodecyl Sulfate; D006859:Hydrogen