The backbone dynamics of the channel-forming peptide antibiotic zervamicin IIB (Zrv-IIB) in methanol were studied by 15N 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 15N 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. © 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Korzhnev, D. M., Bocharov, E. V., Zhuravlyova, A. V., Orekhov, V. Y., Ovchinnikova, T. V., Billeter, M., & Arseniev, A. S. (2001). Backbone dynamics of the channel-forming antibiotic zervamicin IIB studied by 15N NMR relaxation. FEBS Letters, 495(1–2), 52–55. https://doi.org/10.1016/S0014-5793(01)02363-8