Phosphorylated amino acids are highly involved in many cell regulatory networks and many research groups are studying proteins containing these post-translational modifications both experimentally and computationally. Current protein force fields are used to investigate a wide variety of structures and dynamics such as ligand binding, enzyme-reaction mechanisms, and protein folding events. ff14SB and ff19SB are the recommended protein force fields for Amber, but do not contain parameters for phosphorylated amino acids. Therefore, there are no Amber force field parameters that can model these amino acids in the same way as unmodified proteins. This poster will show our work to develop dihedral parameters for the side chains of the most common phosphorylated amino acids following the ff14SB approach, training against QM and MM data for multiple backbone conformations. We also present results of testing on several protein systems. 

Amber parameters for phosphorylated amino acids

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.