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.
High-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of (13)C-Detected NMR Spectroscopy Experiments to Determine Key Observables / I.Bertini; I.C.Felli; L.Gonnelli; M.Vasantha Kumar; R.Pierattelli. - In: CHEMBIOCHEM. - ISSN 1439-4227. - STAMPA. - 12:(2011), pp. 2347-2352. [10.1002/cbic.201100406]
High-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of (13)C-Detected NMR Spectroscopy Experiments to Determine Key Observables
BERTINI, IVANO;FELLI, ISABELLA CATERINA;GONNELLI, LEONARDO;MACHOHALLY VENKATESHAIAH, VASANTHA KUMAR;PIERATTELLI, ROBERTA
2011
Abstract
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.
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