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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

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Spontaneous shrinking: The intrinsically disordered tumor suppressor protein p53 was analyzed by using a combination of ion mobility mass spectrometry and molecular dynamics simulations. Structured p53 subdomains retain their overall topology upon transfer into the gas phase. When intrinsically disordered segments are introduced into the protein sequence, however, the complex spontaneously collapses in the gas phase to a compact conformation.

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