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 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.
Korzhnev
D M
DM
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia.
Bocharov
E V
EV
Zhuravlyova
A V
AV
Orekhov
V Y
VY
Ovchinnikova
T V
TV
Billeter
M
M
Arseniev
A S
AS
D016880:Anisotropy; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D003198:Computer Simulation; D007473:Ion Channels / Q000737:chemistry*; D000432:Methanol / Q000737:chemistry; D008968:Molecular Conformation; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D054848:Peptaibols; D010455:Peptides; D012399:Rotation
D000900:Anti-Bacterial Agents; D007473:Ion Channels; D009587:Nitrogen Isotopes; D054848:Peptaibols; D010455:Peptides; C077077:zervamicin IIB; D000432:Methanol