alexa Identification of in vivo substrates of the chaperonin GroEL.
Chemistry

Chemistry

Journal of Physical Chemistry & Biophysics

Author(s): Houry WA, Frishman D, Eckerskorn C, Lottspeich F, Hartl FU

Abstract Share this page

Abstract The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that GroEL interacts strongly with a well-defined set of approximately 300 newly translated polypeptides, including essential components of the transcription/translation machinery and metabolic enzymes. About one third of these proteins are structurally unstable and repeatedly return to GroEL for conformational maintenance. GroEL substrates consist preferentially of two or more domains with alphabeta-folds, which contain alpha-helices and buried beta-sheets with extensive hydrophobic surfaces. These proteins are expected to fold slowly and be prone to aggregation. The hydrophobic binding regions of GroEL may be well adapted to interact with the non-native states of alphabeta-domain proteins. This article was published in Nature and referenced in Journal of Physical Chemistry & Biophysics

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

  • 5th International Conference and Exhibition on Physical Medicine & Rehabilitation
    Aug 14-16, 2017 Los Angeles, USA
  • 2nd International Conference on Physics
    Aug 28-30, 2017 Brussels, Belgium
  • 5th Global Chemistry Congress
    September 04-06, 2017 London, UK
  • 3rd World Chemistry Conference
    September 11-12, 2017 Dallas, USA
  • Global Conference on Physical Chemistry
    September 18-19, 2017 Dublin, Ireland
  • 2nd International Conference on Applied Chemistry  
    October 16-17, 2017 Toronto, Canada
Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords