help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Biophys. J. BioFAST: First Published July 7, 2006. doi:10.1529/biophysj.106.083899
© 2006 by the Biophysical Society.

A more recent version of this article appeared on October 1, 2006.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
biophysj.106.083899v1
91/7/2399    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhan, L.
Right arrow Articles by Liu, W.-K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhan, L.
Right arrow Articles by Liu, W.-K.

BIOPHYSICAL THEORY AND MODELING

Conformational study of Met-enkephalin based on the ECEPP force fields

Lixin Zhan 1*, Jeff Z. Y. Chen 1 and Wing-Ki Liu 1

1 Department of Physics, University of Waterloo

* To whom correspondence should be addressed. E-mail: lzhan{at}sciborg.uwaterloo.ca.

Submitted on February 22, 2006
Revised on May 1, 2006
Accepted on 12 June 2006


  Abstract
We report a computational study of the small peptide Met-enkephalin based on the ECEPP/2 and ECEPP/3 force fields using the basin paving method. We have located a new global minimum when using the ECEPP/3 force field with peptide angles {omega} fixed at 180°. With this new result, we can conclude that the lowest energy configurations of Met-enkephalin predicted based on all four versions of ECEPP have a classic {gamma}-turn centered at residue Gly3 and a {beta}-turn at residues Gly3-Phe4. However, minor differences between the structures also exist.

Key Words: Monte Carlo, basin paving, global optimization, protein folding






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2006 by the Biophysical Society.