help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Originally published as Biophys J. BioFAST on December 16, 2005.
doi:10.1529/biophysj.105.078154
This Article
Right arrow Full Text
Right arrow Full Text (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 reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
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., Jr.
Biophysical Journal 90:L36-L38 (2006)
© 2006 The Biophysical Society

Importance of the CMAP Correction to the CHARMM22 Protein Force Field: Dynamics of Hen Lysozyme

Matthias Buck *, Sabine Bouguet-Bonnet *, Richard W. Pastor {dagger} and Alexander D. MacKerell, Jr. {ddagger}

* Department of Physiology and Biophysics, Case Western Reserve University, Medical School, Cleveland, Ohio 44106; {dagger} Laboratory of Biophysics, Center for Biologics Evaluation and Research, Food and Drug Administration, Rockville, Maryland 20852; and {ddagger} School of Pharmacy, University of Maryland, Baltimore, Maryland 21201

Correspondence: Address reprint requests and inquiries to Matthias Buck, Tel.: 216-368-8651; Fax: 216-368-1693; E-mail: mxb150{at}case.edu.

The recently developed CMAP correction to the CHARMM22 force field (C22) is evaluated from 25 ns molecular dynamics simulations on hen lysozyme. Substantial deviations from experimental backbone root mean-square 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 molecular dynamics simulations.




This article has been cited by other articles:


Home page
 Biophys. JHome page
Z. Chen, J. Lou, C. Zhu, and K. Schulten
Flow-Induced Structural Transition in the {beta}-Switch Region of Glycoprotein Ib
Biophys. J., August 1, 2008; 95(3): 1303 - 1313.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
A. N. Koller, H. Schwalbe, and H. Gohlke
Starting Structure Dependence of NMR Order Parameters Derived from MD Simulations: Implications for Judging Force-Field Quality
Biophys. J., July 1, 2008; 95(1): L04 - L06.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. Sotomayor and K. Schulten
The Allosteric Role of the Ca2+ Switch in Adhesion and Elasticity of C-Cadherin
Biophys. J., June 15, 2008; 94(12): 4621 - 4633.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. B. Hamaneh and M. Buck
Acceptable Protein and Solvent Behavior in Primary Hydration Shell Simulations of Hen Lysozyme
Biophys. J., April 1, 2007; 92(7): L49 - L51.
[Abstract] [Full Text] [PDF]


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