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- W2515677532 abstract "Cofilin is one of the most essential regulatory proteins and participates in the process of disassembling actin filaments. Cofilin induces conformational changes to actin filaments, and both the bending and torsional rigidity of the filament. In this study, we investigate the effects of cofilin on the mechanical properties of actin filaments using computational methods. Three models defined by their number of bound cofilins are constructed using coarse-grained MARTINI force field, and they are then extended with steered molecular dynamics simulation. After obtaining the stress–strain curves of the models, we calculate their Young's moduli and other mechanical properties that have not yet been determined for actin filaments. We analyze the cause of the different behaviors of the three models based on their atomistic geometrical differences. Finally, it is demonstrated that cofilin binding causes changes in the distances, angles, and stabilities of the residues in actin filaments." @default.
- W2515677532 created "2016-09-16" @default.
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- W2515677532 creator A5013702260 @default.
- W2515677532 creator A5029976028 @default.
- W2515677532 creator A5045329232 @default.
- W2515677532 date "2016-11-01" @default.
- W2515677532 modified "2023-10-17" @default.
- W2515677532 title "Steered molecular dynamics analysis of the role of cofilin in increasing the flexibility of actin filaments" @default.
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- W2515677532 doi "https://doi.org/10.1016/j.bpc.2016.08.002" @default.
- W2515677532 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27589672" @default.
- W2515677532 hasPublicationYear "2016" @default.
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