Backbone dynamics of the channel-forming antibiotic zervamicin IIB studied by 15N NMR relaxation

The backbone dynamics of the channel-forming peptide antibiotic zervamicin IIB (Zrv-IIB) in methanol,were studied by N-15 nuclear magnetic resonance relaxation measurements at 11.7, 14.1 and 18.8 T magnetic fields, The anisotropic overall rotation of the peptide was characterized based on N-15 relaxation data and by hydrodynamic calculations. 'Model-free' analysis of the relaxation data showed that the peptide is fairly rigid on a sub-nanosecond time-scale. The residues from the polar side of Zrv-IIB helix are involved in micro-millisecond time-scale conformational exchange, The conformational exchange observed might indicate intramolecular processes or specific intermolecular interactions of potential relevance to Zrv-IIB ion channel formation. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.