Abstract Background Molecular Mechanics (MM) is the method of choice for computational
studies of biomolecular systems owing to its modest computational cost, which makes it …

Molecular Mechanics (MM) force fields are the methods of choice for protein simulations,
which are essential in the study of conformational flexibility. Given the importance of protein …

While the quality of the current CHARMM22/CMAP additive force field for proteins has been
demonstrated in a large number of applications, limitations in the model with respect to the …

A significant modification to the additive all-atom CHARMM lipid force field (FF) is developed
and applied to phospholipid bilayers with both choline and ethanolamine containing head …

The widely used CHARMM additive all‐atom force field includes parameters for proteins,
nucleic acids, lipids, and carbohydrates. In the present article, an extension of the CHARMM …

We report a reparameterization of the glycosidic torsion χ of the Cornell et al. AMBER force
field for RNA, χOL. The parameters remove destabilization of the anti region found in the ff99 …

The inability to rapidly generate accurate and robust parameters for novel chemical matter
continues to severely limit the application of molecular dynamics simulations to many …

Monosaccharide derivatives such as xylose, fucose, N-acetylglucosamine (GlcNAc), N-
acetylgalactosamine (GlaNAc), glucuronic acid, iduronic acid, and N-acetylneuraminic acid …

Presented is a polarizable force field based on a classical Drude oscillator framework,
currently implemented in the programs CHARMM and NAMD, for modeling and molecular …

We present an extension of the CHARMM hexopyranose monosaccharide additive all-atom
force field to enable modeling of glycosidic-linked hexopyranose polysaccharides. The new …