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• W2971676654 abstract "Molecular dynamics simulations have been performed for a model aqueous solution of mucin. As mucin is a central part of lubricin, a key component of synovial fluid, we investigate its ability to form cross-linked networks. Such network formation could be of major importance for the viscoelastic properties of the soft-matter system and crucial for understanding the lubrication mechanism in articular cartilage. Thus, the inter- and intra-molecular interaction energies between the residues of mucin are analyzed. The results indicate that the mucin concentration significantly impacts its cross-linking behavior. Between 160 g/L and 214 g/L, there seems to be a critical concentration above which crowding begins to alter intermolecular interactions and their energies. This transition is further supported by the mean squared displacement of the molecules. At a high concentration, the system starts to behave subdiffusively due to network development. We also calculate a sample mean squared displacement and p-variation tests to demonstrate how the statistical nature of the dynamics is likewise altered for different concentrations." @default.
• W2971676654 created "2019-09-12" @default.
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• W2971676654 date "2019-09-06" @default.
• W2971676654 modified "2023-10-01" @default.
• W2971676654 title "Formation of Protein Networks between Mucins: Molecular Dynamics Study Based on the Interaction Energy of the System" @default.
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• W2971676654 doi "https://doi.org/10.3390/en12183448" @default.
• W2971676654 hasPublicationYear "2019" @default.
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