Combining coarse-grained nonbonded and atomistic bonded interactions for protein modeling

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Abstract

A hybrid coarse-grained (CG) and atomistic (AT) model for protein simulations and rapid searching and refinement of peptide-protein complexes has been developed. In contrast to other hybrid models that typically represent spatially separate parts of a protein by either a CG or an AT force field model, the present approach simultaneously represents the protein by an AT (united atom) and a CG model. The interactions of the protein main chain are described based on the united atom force field allowing a realistic representation of protein secondary structures. In addition, the AT description of all other bonded interactions keeps the protein compatible with a realistic bonded geometry. Nonbonded interactions between side chains and side chains and main chain are calculated at the level of a CG model using a knowledge-based potential. Unrestrained molecular dynamics simulations on several test proteins resulted in trajectories in reasonable agreement with the corresponding experimental structures. Applications to the refinement of docked peptide-protein complexes resulted in improved complex structures. Application to the rapid refinement of docked protein-protein complex is also possible but requires further optimization of force field parameters.

Original languageEnglish
Pages (from-to)81-92
Number of pages12
JournalProteins: Structure, Function and Bioinformatics
Volume81
Issue number1
DOIs
StatePublished - Jan 2013

Keywords

  • Biased force field
  • Binding site prediction
  • Docking by energy minimization
  • Protein-protein complex formation
  • Protein-protein interaction

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