IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v447y2007i7140d10.1038_nature05728.html
   My bibliography  Save this article

A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein

Author

Listed:
  • K. Hun Mok

    (University of Oxford, Physical & Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK
    School of Biochemistry and Immunology, Trinity College, University of Dublin, Dublin 2, Ireland)

  • Lars T. Kuhn

    (University of Oxford, Physical & Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK)

  • Martin Goez

    (Fachbereich Chemie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 2, D-06120 Halle/Saale, Germany)

  • Iain J. Day

    (University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA
    Present address: Medway Sciences, University of Greenwich, Medway University Campus, Central Avenue, Chatham Maritime, Chatham, Kent, ME4 4TB, UK.)

  • Jasper C. Lin

    (University of Washington, Seattle, Washington 98195, USA)

  • Niels H. Andersen

    (University of Washington, Seattle, Washington 98195, USA)

  • P. J. Hore

    (University of Oxford, Physical & Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK)

Abstract

A nuclear magnetic resonance technique is developed that allows early atomic interactions to be read out later, in the more homogeneous folded state. When this is applied to an ultrafast folding designer protein, it discovers an early hydrophobic core that had been overlooked by computational models.

Suggested Citation

  • K. Hun Mok & Lars T. Kuhn & Martin Goez & Iain J. Day & Jasper C. Lin & Niels H. Andersen & P. J. Hore, 2007. "A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein," Nature, Nature, vol. 447(7140), pages 106-109, May.
    • Handle: RePEc:nat:nature:v:447:y:2007:i:7140:d:10.1038_nature05728
    DOI: 10.1038/nature05728
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature05728
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature05728?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Isabella Daidone & Hannes Neuweiler & Sören Doose & Markus Sauer & Jeremy C Smith, 2010. "Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains," PLOS Computational Biology, Public Library of Science, vol. 6(1), pages 1-9, January.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:447:y:2007:i:7140:d:10.1038_nature05728. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.