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 language | English |
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Pages (from-to) | 81-92 |
Number of pages | 12 |
Journal | Proteins: Structure, Function and Bioinformatics |
Volume | 81 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2013 |
Keywords
- Biased force field
- Binding site prediction
- Docking by energy minimization
- Protein-protein complex formation
- Protein-protein interaction