Direct correlation of consecutive C′–N groups in proteins: a method for the assignment of intrinsically disordered proteins
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Two novel 3D 13C-detected experiments, hNcocaNCO and hnCOcaNCO, are proposed to facilitate the resonance assignment of intrinsically disordered proteins. The experiments correlate the 15N and 13C′ chemical shifts of two consecutive amide moieties without involving other nuclei, thus taking advantage of the good dispersion shown by the 15N–13C′ correlations, even for proteins that lack a well defined tertiary structure. The new pulse sequences were successfully tested using Nupr1, an intrinsically disordered protein of 93 residues.
KeywordsIntrinsically disordered proteins Backbone assignment 13C-detected experiments Multidimensional NMR
This work was supported by project CTQ2011-22514 from the Spanish Ministerio de Economía y Competitividad. The authors thank J.L. Neira (Universidad Miguel Hernández, Alicante, Spain) and J.L. Iovanna (Centre de Recherche en Cancérologie, Marseille, France) for the Nupr1 sample.
- Bermel W, Bertini I, Chill J, Felli IC, Haba N, Kumar V, Pieratelli R (2012b) Exclusively heteronuclear 13C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDP). Chem Biochem 13:2425–2432Google Scholar
- Motácková V, Novácek J, Zawadzka-Kazimierczuk A, Kazimierczuk K, Žídek L, Sanderová H, Krásny L, Kozminski W, Sklenár V (2010) Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution enhanced 5D experiments. J Biomol NMR 48:169–177CrossRefGoogle Scholar