Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase

Authors

  • Dr. Kevin Pagel,

    1. Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, OX1 3QZ, Oxford (UK)
    2. Current address: Department of Molecular Physics, Fritz Haber Institute of the Max Planck Society, Faradayweg 4–6, 14195 Berlin (Germany)
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    • These authors contributed equally to this work.

  • Dr. Eviatar Natan,

    1. MRC Laboratory of Molecular Biology, Hills Road, CB2 0QH, Cambridge (UK)
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    • These authors contributed equally to this work.

  • Zoe Hall,

    1. Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, OX1 3QZ, Oxford (UK)
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  • Prof. Dr. Alan R. Fersht,

    1. MRC Laboratory of Molecular Biology, Hills Road, CB2 0QH, Cambridge (UK)
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  • Prof. Dr. Carol V. Robinson

    Corresponding author
    1. Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, OX1 3QZ, Oxford (UK)
    • Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, OX1 3QZ, Oxford (UK)

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  • We thank J. L. P. Benesch and G. von Helden for critical reading, the German Academy of Sciences Leopoldina (K.P.), The Royal Society (A.R.F., C.V.R.) for support, and an MRC Programme Grant G0901534 to A.R.F.

Abstract

original image

Spontanes Schrumpfen: Das intrinsisch ungeordnete Tumorsuppressorprotein p53 wurde durch Ionenmobilitätsmassenspektrometrie und Moleküldynamiksimulationen untersucht. Strukturierte p53-Unterdomänen behalten ihre Topologie beim Transfer in die Gasphase bei. Werden intrinsisch ungeordnete Segmente in die Proteinsequenz eingeführt, so kollabiert jedoch der Komplex spontan in der Gasphase zu einer kompakten Konformation.

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