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Article

Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling electron paramagnetic resonance spectroscopy.

The journal of physical chemistry. B - 19 Oct 2006

Morin Benjamin, Bourhis Jean-Marie, Belle Valérie, Woudstra Mireille, Carrière Frédéric, Guigliarelli Bruno, Fournel André, Longhi Sonia

Abstract excerpt

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 (N(TAIL)). Four single-site N(TAIL) mutants (S407C, S488C, L496C, and V517C), located in three conserved regions, were prepared and labeled with a nitroxide paramagnetic probe. We could monitor the gain of rigidity that...

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PMID: 17034249
DOI: 10.1021/jp063708u

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