Work

Development of the CHARMM Force Field for Lipids

Year: 2011

Type: article

Abstract: The development of the CHARMM additive all-atom lipid force field (FF) is traced from the early 1990's to the most recent version (C36) published in 2010. Though simulations with early versions yielded useful results, they failed to reproduce two important quantities: a zero surface tension at the experimental bilayer surface area, and the signature splitting of the deuterium order parameters in the glycerol and upper chain carbons. Systematic optimization of parameters based on high level quantum mechanical data and free energy simulations have resolved these issues, and bilayers with a wide range of lipids can be simulated in tensionless ensembles using C36. Issues associated with other all-atom lipid FFs, success and limitations in the C36 FF and ongoing developments are also discussed.

Source: The Journal of Physical Chemistry Letters

DOI: 10.1021/jz200167q

Authors: R. W. Pastor, A. D. MacKerell

Institutions: University of Maryland, Baltimore, National Institutes of Health, National Heart, Lung, and Blood Institute

Language: English

Topic: Lipid Membrane Structure and Behavior

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: Polarizable Force Field for Proteins and Lipids, Oligonucleotide Conformational Heterogeneity, Carbohydrate force fields for structure, dynamics and molecular recognition