Crystallization of asymmetric patchy models for globular proteins in solution.
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Asymmetric patchy particle models have recently been shown to describe the crystallization of small globular proteins with near-quantitative accuracy. Here, we investigate how asymmetry in patch geometry and bond energy generally impacts the phase diagram and nucleation dynamics of this family of soft matter models. We find the role of the geometry asymmetry to be weak, but the energy asymmetry to markedly interfere with the crystallization thermodynamics and kinetics. These results provide a rationale for the success and occasional failure of the proposal of George and Wilson for protein crystallization conditions as well as physical guidance for developing more effective protein crystallization strategies.
Published Version (Please cite this version)10.1103/PhysRevE.88.012721
Publication InfoCharbonneau, Patrick; & Fusco, Diana (2013). Crystallization of asymmetric patchy models for globular proteins in solution. Phys Rev E Stat Nonlin Soft Matter Phys, 88(1). pp. 012721. 10.1103/PhysRevE.88.012721. Retrieved from http://hdl.handle.net/10161/12613.
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Associate Professor of Chemistry
Professor Charbonneau studies soft matter. His work combines theory and simulation to understand the glass problem, protein crystallization, microphase formation, and colloidal assembly in external fields.