Secondary Structure Propensities in Peptide Folding Simulations: A Systematic Comparison of Molecular Mechanics Interaction Schemes
Open Access
- 1 July 2009
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 97 (2) , 599-608
- https://doi.org/10.1016/j.bpj.2009.04.061
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- A consensus view of protein dynamicsProceedings of the National Academy of Sciences, 2007
- Comparison of multiple Amber force fields and development of improved protein backbone parametersProteins-Structure Function and Bioinformatics, 2006
- The Solvation Interface is a Determining Factor in Peptide Conformational PreferencesJournal of Molecular Biology, 2005
- GROMACS: Fast, flexible, and freeJournal of Computational Chemistry, 2005
- Empirical force fields for biological macromolecules: Overview and issuesJournal of Computational Chemistry, 2004
- A point‐charge force field for molecular mechanics simulations of proteins based on condensed‐phase quantum mechanical calculationsJournal of Computational Chemistry, 2003
- Essential dynamics of proteinsProteins-Structure Function and Bioinformatics, 1993
- Molecular dynamics with coupling to an external bathThe Journal of Chemical Physics, 1984
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Comparison of simple potential functions for simulating liquid waterThe Journal of Chemical Physics, 1983