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Classical nucleation theory of virus capsids.
- Source :
-
Biophysical journal [Biophys J] 2006 Mar 15; Vol. 90 (6), pp. 1939-48. Date of Electronic Publication: 2005 Dec 30. - Publication Year :
- 2006
-
Abstract
- A fundamental step in the replication of a viral particle is the self-assembly of its rigid shell (capsid) from its constituent proteins. Capsids play a vital role in genome replication and intercellular movement of viruses, and as such, understanding viral assembly has great potential in the development of new antiviral therapies and a systematic treatment of viral infection. In this article, we assume that nucleation is the underlying mechanism for self-assembly and combine the theoretical methods of the physics of equilibrium polymerization with those of the classical nucleation to develop a theory for the kinetics of virus self-assembly. We find expressions for the size of the critical capsid, the lag time, and the steady-state nucleation rate of capsids, and how they depend on both protein concentration and binding energy. The latter is a function of the acidity of the solution, the ionic strength, and the temperature, explaining why capsid nucleation is a sensitive function of the ambient conditions.
- Subjects :
- Binding Sites
Computer Simulation
Crystallization methods
Models, Molecular
Multiprotein Complexes chemistry
Multiprotein Complexes physiology
Protein Binding
Capsid chemistry
Capsid physiology
Capsid Proteins chemistry
Capsid Proteins physiology
Models, Biological
Models, Chemical
Virus Assembly physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3495
- Volume :
- 90
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Biophysical journal
- Publication Type :
- Academic Journal
- Accession number :
- 16387781
- Full Text :
- https://doi.org/10.1529/biophysj.105.072975