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- W4213446001 abstract "Proteins encounter frequent molecular interactions in biological environments. Computer simulations have become an increasingly important tool in providing mechanistic insights into how such interactions in vivo relate to their biological function. The review here focuses on simulations describing protein assembly and molecular crowding effects as two important aspects that are distinguished mainly by how specific and long-lived protein contacts are. On the topic of crowding, recent simulations have provided new insights into how crowding affects protein folding and stability, modulates enzyme activity, and affects diffusive properties. Recent studies of assembly processes focus on assembly pathways, especially for virus capsids, amyloid aggregation pathways, and the role of multivalent interactions leading to phase separation. Also, discussed are technical challenges in achieving increasingly realistic simulations of interactions in cellular environments." @default.
- W4213446001 created "2022-02-25" @default.
- W4213446001 creator A5061800523 @default.
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- W4213446001 date "2022-04-01" @default.
- W4213446001 modified "2023-10-01" @default.
- W4213446001 title "Protein assembly and crowding simulations" @default.
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- W4213446001 doi "https://doi.org/10.1016/j.sbi.2022.102340" @default.
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