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High‐Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of 13 C‐Detected NMR Spectroscopy Experiments to Determine Key Observables
Author(s) -
Bertini Ivano,
Felli Isabella C.,
Gonnelli Leonardo,
Kumar M. Vasantha,
Pierattelli Roberta
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100406
Subject(s) - characterization (materials science) , nuclear magnetic resonance spectroscopy , spectroscopy , observable , intrinsically disordered proteins , resolution (logic) , chemistry , two dimensional nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , crystallography , nanotechnology , materials science , physics , computer science , quantum mechanics , artificial intelligence
Order in disorder: The characterization of intrinsically disordered proteins by NMR spectroscopy is a necessity on the one hand and a continuous challenge on the other. We propose two experiments that provide diagnostic parameters to monitor the degree of unfolding of a polypeptide. The test was performed on the yeast Cox17 protein, known to gain its function through maturation from an intrinsically disordered state (see figure).