Journal
BIOPHYSICAL JOURNAL
Volume 91, Issue 4, Pages 1501-1512Publisher
BIOPHYSICAL SOCIETY
DOI: 10.1529/biophysj.105.072603
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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 our model 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 suggest that these factors could be universal and relevant to a large class of virus coat proteins.
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