Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 113, Issue 12, Pages 3813-3819Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp8079765
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Funding
- U.S. National Science Foundation [CHE 0400363, CHE 0714411]
- CONACYT [60833]
- UC MEXUS-CONACYT Collaborative Grant
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0714411] Funding Source: National Science Foundation
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We present an experimental study of the self-assembly of capsid proteins of the cowpea chlorotic mosaic virus (CCMV), in the absence of the viral genome, as a function of pH and ionic strength. In accord with previous measurements, a wide range of polymorphs can be identified by electron microscopy, among them single and multiwalled shells and tubes. The images are analyzed with respect to size and shape of aggregates, and evidence is given that equilibrium has been achieved, allowing a phase diagram to be constructed. Some previously unreported structures are also described. The range and stability of the polymorphs can be understood in terms of electrostatic interactions and the way they affect the spontaneous curvature of protein networks and the relative stabilities of pentamers and hexamers.
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