IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v438y2005i7068d10.1038_nature04395.html
   My bibliography  Save this article

Solving the membrane protein folding problem

Author

Listed:
  • James U. Bowie

    (UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, Boyer Hall, UCLA)

Abstract

One of the great challenges for molecular biologists is to learn how a protein sequence defines its three-dimensional structure. For many years, the problem was even more difficult for membrane proteins because so little was known about what they looked like. The situation has improved markedly in recent years, and we now know over 90 unique structures. Our enhanced view of the structure universe, combined with an increasingly quantitative understanding of fold determination, engenders optimism that a solution to the folding problem for membrane proteins can be achieved.

Suggested Citation

  • James U. Bowie, 2005. "Solving the membrane protein folding problem," Nature, Nature, vol. 438(7068), pages 581-589, December.
    • Handle: RePEc:nat:nature:v:438:y:2005:i:7068:d:10.1038_nature04395
    DOI: 10.1038/nature04395
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature04395
    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/nature04395?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. Mengke Li & Hongzhi Tang & Rui Qing & Yanze Wang & Jiongqin Liu & Rui Wang & Shan Lyu & Lina Ma & Ping Xu & Shuguang Zhang & Fei Tao, 2024. "Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code," 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:438:y:2005:i:7068:d:10.1038_nature04395. 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.