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- W2912491397 abstract "Proteins with folded domains are quite common in extracellular matrices. Upon loading, mechanical forces will be transmitted down to individual protein chains within the matrices so that their folded domains can be stochastically unfolded or refolded. Such a kinetic process occurring at the molecular level is believed to be crucial to both mechanical properties and physiological functions of native tissues, which has inspired abundant studies in engineering protein hydrogels with folded domains. In most of these studies, an ideal defect-free protein network was often presented to elucidate its mechanical properties. However, defects in the protein network may be inevitable in the fabrication and how they affect mechanical properties of the network is intriguing. As the first step in addressing this issue, the unfolding/refolding kinetics of the protein domains changed by the defects are considered and implemented to a network model to analyze the viscoelasticity of protein hydrogels. The analysis indicates that fractions of folded domains with altered unfolding/folding kinetics within the network can strongly affect the viscoelasticity of the protein network. This theoretical work also recovers peculiar features in the loading and unloading curve for protein hydrogels reported in experiments. The comparison between theory and experiments suggests that there exist certain number of defects in fabricated protein hydrogels." @default.
- W2912491397 created "2019-02-21" @default.
- W2912491397 creator A5034166563 @default.
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- W2912491397 date "2019-04-01" @default.
- W2912491397 modified "2023-10-13" @default.
- W2912491397 title "Constitutive model reveals the defect-dependent viscoelasticity of protein hydrogels" @default.
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- W2912491397 doi "https://doi.org/10.1016/j.jmps.2019.01.015" @default.
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