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

FEBS Letters

Bocharov, Eduard V¹  Ovchinnikova, Tatyana V¹  Arseniev, Alexander S¹  Korzhnev, Dmitry M¹  Billeter, Martin²  Orekhov, Vladislav Yu²  Zhuravlyova, Anastasya V¹ 

[1] Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia;Swedish NMR Center at Göteborg University, P.O. Box 465, 405 30 Göteborg, Sweden

关键词: Peptaibol;    Dynamics;    Anisotropy;    Model-free;    Conformational exchange;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;    CPMG;    Carr Pursell Meiboom Gill;    CSA;    chemical shift anisotropy;    Zrv-IIB;    zervamicin IIB;   

DOI  :  10.1016/S0014-5793(01)02363-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown