Step-wise thermal denaturation of cobrotoxin, a snake venom neurotoxin from Naja naja atra: a proton nuclear magnetic resonance study.
Temperature dependence of proton nuclear magnetic resonance spectra has been followed for cobrotoxin, a postsynaptic neurotoxin from Naja naja atra venom. Several aromatic amino-acid residues, including the functionally essential Trp-29 located at the tip of the central loop of the molecule, have been found to undergo a thermal structural transition above the global thermal denaturation temperature. It is suggested that a local structure around these residues behaves somehow independently of the rest of the molecule, and that such structural organization may be favorable for a conformational change of a neurotoxin molecule on binding to acetylcholine receptor.
Endo
T
T
Department of Chemistry, College of Technology, Gunma University, Kiryu, Japan.
Oya
M
M
Hayashi
K
K
Miyazawa
T
T
D003039:Cobra Neurotoxin Proteins; D004546:Elapid Venoms; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D011489:Protein Denaturation
D003039:Cobra Neurotoxin Proteins; D004546:Elapid Venoms