During the replication of many viruses, hundreds to thousands of proteins assemble around the viral nucleic acid to form a protein shell called a capsid. We focus on understanding the role of the encapsidated RNA, DNA, or man-made cargoes such as drugs or functionalized nanoparticles, in the capsid assembly process. Interactions with a nucleic acid core or other cargo can direct assembly in many ways, ranging from the simple physical size of the core, to electrostatics, to sequence-specific interactions between capsid proteins and/or nucleotides. To determine the influence of each of these factors on assembly, we have systematically studied assembly around different types of cargoes, ranging from no cargo (empty capsids) to rigid nanoparticles to flexible polymers, to polymers with architectures which represent base pairing. At the same time, we are progressively building more realistic representations of capsid proteins, in part by studying their conformations in atomic-resolution simulations. At each stage of complexity, we obtain model predictions that can be compared to experiments on capsid assembly around functionalized nanoparticles, synthetic polyelectrolytes, or nucleic acids. Some of the projects we have pursued are described in more detail in the following links.
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