High-resolution characterization of intrinsic disorder in proteins: expanding the suite of (13)C-detected NMR spectroscopy experiments to determine key observables.

Autor: Bertini I; CERM University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy. ivanobertini@cerm.unifi.it, Felli IC, Gonnelli L, Vasantha Kumar MV, Pierattelli R
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2011 Oct 17; Vol. 12 (15), pp. 2347-52.
DOI: 10.1002/cbic.201100406
Abstrakt: 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).
Databáze: MEDLINE