Oxidative Folding Intermediates with Nonnative Disulfide Bridges between Adjacent Cysteine Residues

The oxidative folding of the Amaranthus α-amylase inhibitor, a 32-residue cystine-knot protein with three disulfide bridges, was studied in vitro in terms of the disulfide content of the intermediate species. A nonnative vicinal disulfide bridge between cysteine residues 17 and 18 was found in three...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2003-05, Vol.100 (10), p.5754-5759
Hauptverfasser:	Čemažar, Maša, Zahariev, Sotir, Lopez, Jakob J., Carugo, Oliviero, Jones, Jonathan A., Hore, P. J., Pongor, Sándor
Format:	Artikel
Sprache:	eng
Schlagworte:	alpha-Amylases - antagonists & inhibitors Biochemistry Biological Sciences Bridge engineering Chemical equilibrium Cysteine Databases, Factual Disulfides Hydrodynamics Magnetic Resonance Spectroscopy Mathematical rings Models, Molecular Molecular structure Nonnative species Oxidation Oxidation-Reduction Plant Proteins - chemistry Plant Proteins - metabolism Protein Conformation Protein Folding Protein Structure, Secondary Spectral resolution Spectroscopy Sulfide compounds Topology Trypsin Inhibitors
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