IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v465y2010i7298d10.1038_nature09021.html
   My bibliography  Save this article

The folding cooperativity of a protein is controlled by its chain topology

Author

Listed:
  • Elizabeth A. Shank

    (University of California, Berkeley, California 94720, USA
    Jason L. Choy Laboratory of Single Molecule Biophysics, Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, USA
    Present addresses: Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA (E.A.S.); Department of Physics, University of Modena and Reggio Emilia, Via Campi 213/A 4100 Modena, Italy (C.C.).)

  • Ciro Cecconi

    (University of California, Berkeley, California 94720, USA
    Jason L. Choy Laboratory of Single Molecule Biophysics, Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, USA
    Present addresses: Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA (E.A.S.); Department of Physics, University of Modena and Reggio Emilia, Via Campi 213/A 4100 Modena, Italy (C.C.).)

  • Jesse W. Dill

    (Jason L. Choy Laboratory of Single Molecule Biophysics, Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, USA
    Biophysics Graduate Group, University of California, Berkeley, California 94720, USA)

  • Susan Marqusee

    (University of California, Berkeley, California 94720, USA
    Jason L. Choy Laboratory of Single Molecule Biophysics, Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, USA)

  • Carlos Bustamante

    (University of California, Berkeley, California 94720, USA
    Jason L. Choy Laboratory of Single Molecule Biophysics, Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, USA
    Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA
    University of California, Berkeley, California 94720, USA)

Abstract

Into the fold: protein domains reshuffled Protein molecules often include domains that can be distinguished as relatively separate regions in their three-dimensional structure, but how such domains communicate during folding or enzymatic function is largely unclear. Shank et al. have now developed a new technology to study this using single-molecule optical tweezers acting via DNA 'handles' to pull on a protein from different directions while monitoring the energetics of unfolding and refolding events in regions away from those submitted to mechanical forces. Comparing topological variants of a protein — the two-domain protein T4 lysozyme that is a familiar model for folding studies — they then derive new rules of cooperation between sub-domains and suggest how evolution may select reshuffled gene topologies that bypass folding dead-ends.

Suggested Citation

  • Elizabeth A. Shank & Ciro Cecconi & Jesse W. Dill & Susan Marqusee & Carlos Bustamante, 2010. "The folding cooperativity of a protein is controlled by its chain topology," Nature, Nature, vol. 465(7298), pages 637-640, June.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7298:d:10.1038_nature09021
    DOI: 10.1038/nature09021
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09021
    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/nature09021?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. Jaka Vodeb & Michele Diego & Yevhenii Vaskivskyi & Leonard Logaric & Yaroslav Gerasimenko & Viktor Kabanov & Benjamin Lipovsek & Marko Topic & Dragan Mihailovic, 2024. "Non-equilibrium quantum domain reconfiguration dynamics in a two-dimensional electronic crystal and a quantum annealer," Nature Communications, Nature, vol. 15(1), pages 1-7, December.
    2. Seth Lichter & Benjamin Rafferty & Zachary Flohr & Ashlie Martini, 2012. "Protein High-Force Pulling Simulations Yield Low-Force Results," PLOS ONE, Public Library of Science, vol. 7(4), pages 1-10, April.
    3. Sahar Foroutannejad & Lydia L. Good & Changfan Lin & Zachariah I. Carter & Mahlet G. Tadesse & Aaron L. Lucius & Brian R. Crane & Rodrigo A. Maillard, 2023. "The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    4. Willow Coyote-Maestas & David Nedrud & Antonio Suma & Yungui He & Kenneth A. Matreyek & Douglas M. Fowler & Vincenzo Carnevale & Chad L. Myers & Daniel Schmidt, 2021. "Probing ion channel functional architecture and domain recombination compatibility by massively parallel domain insertion profiling," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    5. Ganesh Agam & Anders Barth & Don C. Lamb, 2024. "Folding pathway of a discontinuous two-domain protein," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

    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:465:y:2010:i:7298:d:10.1038_nature09021. 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.