Theoretical aspects of virus capsid assembly
- 29 September 2005
- journal article
- review article
- Published by Wiley in Journal of Molecular Recognition
- Vol. 18 (6), 479-490
- https://doi.org/10.1002/jmr.754
Abstract
A virus capsid is constructed from many copies of the same protein(s). Molecular recognition is central to capsid assembly. The capsid protein must polymerize in order to create a three‐dimensional protein polymer. More than structure is required to understand this self‐assembly reaction: one must understand how the pieces come together in solution. Copyright © 2005 John Wiley & Sons, Ltd.Keywords
This publication has 82 references indexed in Scilit:
- Regulating Self-Assembly of Spherical OligomersNano Letters, 2005
- Three-dimensional Structure of HIV-1 Virus-like Particles by Electron CryotomographyJournal of Molecular Biology, 2005
- The energy landscape as a unifying theme in molecular sciencePhilosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences, 2004
- Supramolecular self-assembly: molecular dynamics modeling of polyhedral shell formationComputer Physics Communications, 1999
- Local Rules Simulation of the Kinetics of Virus Capsid Self-AssemblyBiophysical Journal, 1998
- Conserved Features in Papillomavirus and Polyomavirus CapsidsJournal of Molecular Biology, 1996
- Assembly of T7 Capsids from Independently Expressed and Purified Head Protein and Scaffolding ProteinJournal of Molecular Biology, 1996
- Solvation energy in protein folding and bindingNature, 1986
- The detection of sub-units within the crystallographic asymmetric unitActa Crystallographica, 1962
- Physical Principles in the Construction of Regular VirusesCold Spring Harbor Symposia on Quantitative Biology, 1962