IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v405y2000i6782d10.1038_35011000.html
   My bibliography  Save this article

A surprising simplicity to protein folding

Author

Listed:
  • David Baker

    (University of Washington)

Abstract

The polypeptide chains that make up proteins have thousands of atoms and hence millions of possible inter-atomic interactions. It might be supposed that the resulting complexity would make prediction of protein structure and protein-folding mechanisms nearly impossible. But the fundamental physics underlying folding may be much simpler than this complexity would lead us to expect: folding rates and mechanisms appear to be largely determined by the topology of the native (folded) state, and new methods have shown great promise in predicting protein-folding mechanisms and the three-dimensional structures of proteins.

Suggested Citation

  • David Baker, 2000. "A surprising simplicity to protein folding," Nature, Nature, vol. 405(6782), pages 39-42, May.
  • Handle: RePEc:nat:nature:v:405:y:2000:i:6782:d:10.1038_35011000
    DOI: 10.1038/35011000
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35011000
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/35011000?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. Omar Haq & Michael Andrec & Alexandre V Morozov & Ronald M Levy, 2012. "Correlated Electrostatic Mutations Provide a Reservoir of Stability in HIV Protease," PLOS Computational Biology, Public Library of Science, vol. 8(9), pages 1-10, September.
    2. Yaman Arkun & Burak Erman, 2010. "Prediction of Optimal Folding Routes of Proteins That Satisfy the Principle of Lowest Entropy Loss: Dynamic Contact Maps and Optimal Control," PLOS ONE, Public Library of Science, vol. 5(10), pages 1-11, October.
    3. Yaman Arkun & Mert Gur, 2012. "Combining Optimal Control Theory and Molecular Dynamics for Protein Folding," PLOS ONE, Public Library of Science, vol. 7(1), pages 1-8, January.
    4. Marwa Mohammed M. Ghareeb & Ahmed Sharaf Eldin & Taysir Hassan A. Soliman & Mohammed Ebrahim Marie, 2013. "A Deeply Glimpse into Protein Fold Recognition," International Journal of Sciences, Office ijSciences, vol. 2(06), pages 24-33, June.
    5. Stefano Zamuner & Flavio Seno & Antonio Trovato, 2022. "Statistical potentials from the Gaussian scaling behaviour of chain fragments buried within protein globules," PLOS ONE, Public Library of Science, vol. 17(1), pages 1-20, January.
    6. 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.
    7. Christopher A Brown & Kevin S Brown, 2010. "Validation of Coevolving Residue Algorithms via Pipeline Sensitivity Analysis: ELSC and OMES and ZNMI, Oh My!," PLOS ONE, Public Library of Science, vol. 5(6), pages 1-14, June.
    8. Amit K Chattopadhyay & Biswajit Debnath & Rihab El-Hassani & Sadhan Kumar Ghosh & Rahul Baidya, 2020. "Cleaner Production in Optimized Multivariate Networks: Operations Management through a Roll of Dice," Papers 2003.00884, arXiv.org.

    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:405:y:2000:i:6782:d:10.1038_35011000. 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.