Article ; Online: Structure and energetics guide dynamic behaviour in a T = 3 icosahedral virus capsid.
2023 Volume 305, Page(s) 107152
Abstract: Although virus capsids appear as rigid, symmetric particles in experimentally determined structures; biochemical studies suggest a significant degree of structural flexibility in the particles. We carried out all-atom simulations on the icosahedral ... ...
Abstract | Although virus capsids appear as rigid, symmetric particles in experimentally determined structures; biochemical studies suggest a significant degree of structural flexibility in the particles. We carried out all-atom simulations on the icosahedral capsid of an insect virus, Flock House Virus, which show intriguing differences in the degree of flexibility of quasi-equivalent capsid subunits consistent with previously described biological behaviour. The flexibility of all the β and γ subunits of the protein and RNA fragments is analysed and compared. Both γ |
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MeSH term(s) | Capsid/chemistry ; Capsid/metabolism ; Interleukin Receptor Common gamma Subunit/analysis ; Interleukin Receptor Common gamma Subunit/metabolism ; Capsid Proteins/analysis ; Capsid Proteins/metabolism ; RNA/metabolism ; Water/metabolism |
Chemical Substances | Interleukin Receptor Common gamma Subunit ; Capsid Proteins ; RNA (63231-63-0) ; Water (059QF0KO0R) |
Language | English |
Publishing date | 2023-12-08 |
Publishing country | Netherlands |
Document type | Journal Article ; Research Support, Non-U.S. Gov't |
ZDB-ID | 185052-0 |
ISSN | 1873-4200 ; 0301-4622 |
ISSN (online) | 1873-4200 |
ISSN | 0301-4622 |
DOI | 10.1016/j.bpc.2023.107152 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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