<?xml version="1.0" encoding="UTF-8"?>
<XML><RECORDS>
<RECORD>
	<REFERENCE_TYPE>0</REFERENCE_TYPE>
	<AUTHORS>
		<AUTHOR>Bruinsma, RF</AUTHOR>
		<AUTHOR>Gelbart, WM</AUTHOR>
		<AUTHOR>Reguera, D</AUTHOR>
		<AUTHOR>Rudnick, J</AUTHOR>
		<AUTHOR>Zandi, R</AUTHOR>
	</AUTHORS>
	<YEAR>2003</YEAR>
	<TITLE>Viral self-assembly as a thermodynamic process</TITLE>
	<SECONDARY_TITLE>PHYSICAL REVIEW LETTERS</SECONDARY_TITLE>
	<VOLUME>90</VOLUME>
	<DATE>JUN 20</DATE>
	<KEYWORDS>
		<KEYWORD>COWPEA</KEYWORD>
		<KEYWORD>CHLOROTIC</KEYWORD>
		<KEYWORD>MOTTLE,</KEYWORD>
		<KEYWORD>ICOSAHEDRAL</KEYWORD>
		<KEYWORD>VIRUSES,</KEYWORD>
		<KEYWORD>MOSAIC</KEYWORD>
		<KEYWORD>VIRUS,</KEYWORD>
		<KEYWORD>PLANT-VIRUS,</KEYWORD>
		<KEYWORD>BETA-VIRUS,</KEYWORD>
		<KEYWORD>PROTEIN,</KEYWORD>
		<KEYWORD>PARTICLES,</KEYWORD>
		<KEYWORD>PACKING,</KEYWORD>
		<KEYWORD>CIRCLES,</KEYWORD>
		<KEYWORD>SPHERE</KEYWORD>
	</KEYWORDS>
	<ABSTRACT>&lt;p&gt;The protein shells, or capsids, of nearly all spherelike viruses adopt icosahedral symmetry. In the present Letter, we propose a statistical thermodynamic model for viral self-assembly. We find that icosahedral symmetry is not expected for viral capsids constructed from structurally identical protein subunits and that this symmetry requires (at least) two internal &amp;quot;switching&amp;quot; configurations of the protein. Our results indicate that icosahedral symmetry is not a generic consequence of free energy minimization but requires optimization of internal structural parameters of the capsid proteins.&lt;/p&gt;</ABSTRACT>
	<URL>http://dx.doi.org/10.1103/PhysRevLett.90.248101</URL>
</RECORD>
</RECORDS></XML>