Article ; Online: Virtual indentation of the empty capsid of the minute virus of mice using a minimal coarse-grained model.
2024 Volume 109, Issue 2-1, Page(s) 24402
Abstract: A minimal coarse-grained model for T=1 viral capsids assembled from 20 protein rigid trimers has been designed by extending a previously proposed form of the interaction energy written as a sum of anisotropic pairwise interactions between the trimeric ... ...
| Abstract | A minimal coarse-grained model for T=1 viral capsids assembled from 20 protein rigid trimers has been designed by extending a previously proposed form of the interaction energy written as a sum of anisotropic pairwise interactions between the trimeric capsomers. The extension of the model has been performed to properly account for the coupling between two internal coordinates: the one that measures the intercapsomer distance and the other that gives the intercapsomer dihedral angle. The model has been able to fit with less than a 10% error the atomic force microscopy (AFM) indentation experimental data for the empty capsid of the minute virus of mice (MVM), providing in this way an admissible picture of the main mechanisms behind the capsid deformations. In this scenario, the bending of the intercapsomer dihedral angle is the angular internal coordinate that can support larger deformations away from its equilibrium values, determining important features of the AFM indentation experiments as the elastic constants along the three symmetry axes of the capsid and the critical indentations. From the value of one of the parameters of our model, we conclude that trimers in the MVM must be quite oblate tops, in excellent agreement with their known structure. The transition from the linear to the nonlinear regimes sampled in the indentation process appears to be an interesting topic for future research in physical virology. |
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| MeSH term(s) | Animals ; Mice ; Capsid/chemistry ; Minute Virus of Mice ; Capsid Proteins/chemistry ; Viruses ; Microscopy, Atomic Force |
| Chemical Substances | Capsid Proteins |
| Language | English |
| Publishing date | 2024-03-15 |
| Publishing country | United States |
| Document type | Journal Article |
| ZDB-ID | 2844562-4 |
| ISSN | 2470-0053 ; 2470-0045 |
| ISSN (online) | 2470-0053 |
| ISSN | 2470-0045 |
| DOI | 10.1103/PhysRevE.109.024402 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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