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Biophys. J. BioFAST: First Published May 26, 2006. doi:10.1529/biophysj.105.072603
© 2006 by the Biophysical Society.

A more recent version of this article appeared on August 15, 2006.
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SUPRAMOLECULAR ASSEMBLIES

Physical regulation of the self-assembly of tobacco mosaic virus coat protein

Willem K Kegel 1* and Paul van der Schoot 2

1 Utrecht University
2 Eindhoven University

* To whom correspondence should be addressed. E-mail: w.k.kegel{at}chem.uu.nl.

Submitted on August 12, 2005
Revised on November 12, 2005
Accepted on 9 May 2006


  Abstract
We present a statistical mechanical model based on the principle of mass action that explains the main features of the in vitro aggregation behavior of the coat protein of Tobacco Mosaic Virus (TMV). By comparing to experimentally obtained stability diagrams, titration experiments, and calorimetric data, we pin down three competing factors that regulate the transitions between the different kinds of aggregated state of the coat protein. These are hydrophobic interactions, electrostatic interactions, and the formation of so-called 'Caspar' carboxylate pairs. We put forward that these factors could be universal, and relevant to a large class of virus coat protein.

Key Words: coarse-grained interactions, potential of mean force, self-assembly, tobacco mosaic virus coat protein






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Copyright © 2006 by the Biophysical Society.