Journal of Biomolecular NMR

, Volume 57, Issue 1, pp 57–63 | Cite as

Direct correlation of consecutive C′–N groups in proteins: a method for the assignment of intrinsically disordered proteins

  • David Pantoja-Uceda
  • Jorge SantoroEmail author


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.


Intrinsically 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.


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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  1. 1.Instituto de Química Física RocasolanoCSICMadridSpain

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