Abstract
We report a study of the structural dynamics of viral capsids, simulated on a microsecond timescale, by employing a coarse-graining molecular dynamics method. The method was calibrated against an all-atom simulation of one complete virus. Among the studied capsids, some collapsed rapidly, while others were found to be stable. Interlocking between coat proteins is found to be a key factor determining the stability of the capsids.
Publication types
- Research Support, N.I.H., Extramural
- Research Support, Non-U.S. Gov't
MeSH terms
- Biochemistry / methods*
- Calibration
- Capsid / chemistry*
- Capsid / metabolism
- Computational Biology / methods
- Computer Simulation
- Computers
- Models, Molecular
- Models, Statistical
- Molecular Conformation
- Protein Binding
- Protein Conformation
- Time Factors
- User-Computer Interface
- Viral Proteins / chemistry*
- Viral Proteins / metabolism