help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Biophys. J. BioFAST: First Published December 16, 2005. doi:10.1529/biophysj.105.078154
© 2005 by the Biophysical Society.

A more recent version of this article appeared on February 15, 2006.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow Supplemental
Right arrow All Versions of this Article:
biophysj.105.078154v1
90/4/L36    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 Author home page(s):
Matthias Buck
Alexander D MacKerell
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Buck, M.
Right arrow Articles by MacKerell, A. D
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Buck, M.
Right arrow Articles by MacKerell, A. D

BIOPHYSICAL LETTERS

Importance of the CMAP correction to the CHARMM22 Protein Force Field: dynamics of hen lysozyme

Matthias Buck 1*, Sabine Bonnet 2, Richard W Pastor 3 and Alexander D MacKerell 4

1 Case Western Reserve Univ. Med. School
2 Case Western Reserve University
3 Cntr Biologics Eval. and Research, FDA
4 Univ. of Maryland

* To whom correspondence should be addressed. E-mail: mxb150{at}po.cwru.edu.

Submitted on November 18, 2005
Revised on December 1, 2005
Accepted on 12 December 2005


  Abstract
The recently developed CMAP correction to the CHARMM22 forcefield (C22) is evaluated from 25 ns MD simulations on hen lysozyme. Substantial deviations from experimental backbone RMS fluctuations and N-H NMR order parameters obtained in the C22 trajectories (especially in the loops) are eliminated by the CMAP correction. Thus, the C22/CMAP force field yields improved dynamical and structural properties of proteins in MD simulations.

Key Words: NMR relaxation order parameters, crystallographic B-factors, molecular dynamics simulation, protein force-field, protein internal dynamics






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2005 by the Biophysical Society.