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.





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Fusco, Diana, and Patrick Charbonneau (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

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Patrick Charbonneau

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.

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