Competition between monomeric and dimeric crystals in schematic models for globular proteins.
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Advances in experimental techniques and in theoretical models have improved our understanding of protein crystallization. However, they have also left open questions regarding the protein phase behavior and self-assembly kinetics, such as why (nearly) identical crystallization conditions can sometimes result in the formation of different crystal forms. Here, we develop a patchy particle model with competing sets of patches that provides a microscopic explanation of this phenomenon. We identify different regimes in which one or two crystal forms can coexist with a low-density fluid. Using analytical approximations, we extend our findings to different crystal phases, providing a general framework for treating protein crystallization when multiple crystal forms compete. Our results also suggest different experimental routes for targeting a specific crystal form, and for reducing the dynamical competition between the two forms, thus facilitating protein crystal assembly.
Published Version (Please cite this version)10.1021/jp5011428
Publication InfoCharbonneau, Patrick; & Fusco, Diana (2014). Competition between monomeric and dimeric crystals in schematic models for globular proteins. J Phys Chem B, 118(28). pp. 8034-8041. 10.1021/jp5011428. Retrieved from http://hdl.handle.net/10161/15343.
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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.