Assessing Induced Folding of an Intrinsically Disordered Protein by Site-Directed Spin-Labeling Electron Paramagnetic Resonance Spectroscopy

We used site-directed spin-labeling electron paramagnetic resonance (EPR) spectroscopy to study the induced folding of the intrinsically disordered C-terminal domain of measles virus nucleoprotein (NTAIL). Four single-site NTAIL mutants (S407C, S488C, L496C, and V517C), located in three conserved re...

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Veröffentlicht in:	The journal of physical chemistry. B 2006-10, Vol.110 (41), p.20596-20608
Hauptverfasser:	Morin, Benjamin, Bourhis, Jean-Marie, Belle, Valérie, Woudstra, Mireille, Carrière, Frédéric, Guigliarelli, Bruno, Fournel, André, Longhi, Sonia
Format:	Artikel
Sprache:	eng
Schlagworte:	Biophysics - methods Chemistry, Physical - methods Electron Spin Resonance Spectroscopy Escherichia coli - metabolism Magnetics Molecular Conformation Mutation Nitric Oxide - chemistry Phosphoproteins - chemistry Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Proteins - chemistry Spin Labels
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