• Open Access

Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation

Authors

  • Jan Stanek,

    1. Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw (Poland)
    Search for more papers by this author
  • Saurabh Saxena,

    1. Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw (Poland)
    Search for more papers by this author
  • Leonhard Geist,

    1. Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna (Austria)
    Search for more papers by this author
  • Prof. Robert Konrat,

    Corresponding author
    1. Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna (Austria)
    • Robert Konrat, Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna (Austria)

      Wiktor Koźmiński, Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw (Poland)

    Search for more papers by this author
  • Prof. Wiktor Koźmiński

    Corresponding author
    1. Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw (Poland)
    • Robert Konrat, Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna (Austria)

      Wiktor Koźmiński, Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw (Poland)

    Search for more papers by this author

  • The expression plasmids for wild-type BASP1 were provided by the group of K. Bister (University of Innsbruck). This work was supported by the Austrian Science Foundation (FWF) grants (P20549-N19 and W-1221-B03 to R.K.). The research was co-financed by Bio-NMR Project No. 161863 funded by European Commission’s Framework Program 7 (FP7), as well as by the grant No. 2012/05/N/ST4/01120 funded by Polish National Science Centre. S.S. and W.K. thank the Foundation for Polish science for financial support with the TEAM programme.

Abstract

original image

Hochauflösende NMR-Messungen der Interferenz zwischen 1H(i)-15N(i)-13C′(i)-Dipoleffekten und der Anisotropie der chemischen Verschiebung einzelner Aminosäurepositionen liefern Informationen über lokale Rückgratstrukturen in intrinsisch fehlgeordneten Proteinen. Eine Untersuchung des Tumorsuppressors BASP1 ergab eine Populationsveränderung der β-Schleifen-Strukturen bei tiefen pH-Werten und eine Komprimierung des BASP1-Strukturensembles.

Ancillary