IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v528y2015i7583d10.1038_nature16162.html
   My bibliography  Save this article

Exploring the repeat protein universe through computational protein design

Author

Listed:
  • TJ Brunette

    (University of Washington
    Institute for Protein Design, University of Washington)

  • Fabio Parmeggiani

    (University of Washington
    Institute for Protein Design, University of Washington)

  • Po-Ssu Huang

    (University of Washington
    Institute for Protein Design, University of Washington)

  • Gira Bhabha

    (UCSF)

  • Damian C. Ekiert

    (UCSF)

  • Susan E. Tsutakawa

    (Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley National Laboratory)

  • Greg L. Hura

    (Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley National Laboratory
    University of California)

  • John A. Tainer

    (Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley National Laboratory
    The University of Texas M. D. Anderson Cancer Center)

  • David Baker

    (University of Washington
    Institute for Protein Design, University of Washington
    Howard Hughes Medical Institute, University of Washington)

Abstract

In this study, 83 proteins containing helix–loop–helix–loop repeats were designed—with sequences unrelated to known repeat proteins—and experimentally characterized; 43 solution X-ray scattering spectra and 15 structures of the designed proteins show that these non-natural repeat proteins have a broad range of curvatures and that their overall structures are in close agreement with design models.

Suggested Citation

  • TJ Brunette & Fabio Parmeggiani & Po-Ssu Huang & Gira Bhabha & Damian C. Ekiert & Susan E. Tsutakawa & Greg L. Hura & John A. Tainer & David Baker, 2015. "Exploring the repeat protein universe through computational protein design," Nature, Nature, vol. 528(7583), pages 580-584, December.
  • Handle: RePEc:nat:nature:v:528:y:2015:i:7583:d:10.1038_nature16162
    DOI: 10.1038/nature16162
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature16162
    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/nature16162?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. Thomas W. Linsky & Kyle Noble & Autumn R. Tobin & Rachel Crow & Lauren Carter & Jeffrey L. Urbauer & David Baker & Eva-Maria Strauch, 2022. "Sampling of structure and sequence space of small protein folds," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Fatima A. Davila-Hernandez & Biao Jin & Harley Pyles & Shuai Zhang & Zheming Wang & Timothy F. Huddy & Asim K. Bera & Alex Kang & Chun-Long Chen & James J. Yoreo & David Baker, 2023. "Directing polymorph specific calcium carbonate formation with de novo protein templates," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    3. Fabian Sesterhenn & Che Yang & Jaume Bonet & Johannes T. Cramer & Xiaolin Wen & Yimeng Wang & Chi I. Chiang & Luciano Andres Abriata & Iga Kucharska & Giacomo Castoro & Sabrina S. Vollers & Marie Gall, 2020. "De novo protein design enables the precise induction of RSV-neutralizing antibodies," Post-Print hal-02677103, HAL.

    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:528:y:2015:i:7583:d:10.1038_nature16162. 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.