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Reshaping of the conformational search of a protein by the chaperone trigger factor

Author

Listed:
  • Alireza Mashaghi

    (FOM institute AMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands)

  • Günter Kramer

    (Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, Heidelberg 69120, Germany)

  • Philipp Bechtluft

    (FOM institute AMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands)

  • Beate Zachmann-Brand

    (Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, Heidelberg 69120, Germany)

  • Arnold J. M. Driessen

    (Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 7, 9749 AG Groningen, The Netherlands)

  • Bernd Bukau

    (Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, Heidelberg 69120, Germany)

  • Sander J. Tans

    (FOM institute AMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands)

Abstract

The bacterial chaperone named trigger factor is found to stabilize protein folding intermediates that eventually convert to the native state, suggesting that chaperones play a direct role in instructing protein folding.

Suggested Citation

  • Alireza Mashaghi & Günter Kramer & Philipp Bechtluft & Beate Zachmann-Brand & Arnold J. M. Driessen & Bernd Bukau & Sander J. Tans, 2013. "Reshaping of the conformational search of a protein by the chaperone trigger factor," Nature, Nature, vol. 500(7460), pages 98-101, August.
  • Handle: RePEc:nat:nature:v:500:y:2013:i:7460:d:10.1038_nature12293
    DOI: 10.1038/nature12293
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