• 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)
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  • Saurabh Saxena,

    1. Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw (Poland)
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  • Leonhard Geist,

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

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  • 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)

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  • 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

An ultra-high-resolution NMR experiment for the measurement of intraresidue 1H(i)–15N(i)–13C′(i) dipolar–chemical shift anisotropy relaxation interference is employed to extract information about local backbone geometries in intrinsically disordered proteins. The study of tumor suppressor BASP1 revealed a population shift of β-turn geometries at low pH conditions and a compaction of the BASP1 structural ensemble.

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