Effects of ph and nacl on the spatial structure and conformation of myofibrillar proteins and the emulsion gel system—insights from computational molecular dynamics on myosin of golden pompano

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SUMMARY

    The lack of product diversification underutilizes the fish, which is rich in polyunsaturated_fatty_acids and has a balanced ratio of amino_acids. The solubility of myofibrillar protein is not only related to the protein structure but also to pH, ionic strength, temperature, and protein concentration as well. Due to the amphipathic nature of myofibrillar proteins, the hydrogen_bonds and electrostatic and hydrophobic forces within the protein change in response to its surrounding environment, adopting a new equilibrium structure that leads to changes in its functional properties. Changes in pH can affect the charge distribution of amino_acid side . . .

     

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