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

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Abstract

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.

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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

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