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- W4386150907 abstract "In liquid water, there is a natural tendency to form aggregates that consist of water molecules linked by hydrogen bonds. Such spontaneously formed aggregates are surrounded by a “sea” of disordered water molecules, with both forms remaining in equilibrium. The process of creating water aggregates also takes place in the solvation water of proteins, but in this case, the interactions of water molecules with the protein surface shift the equilibrium of the process. In this paper, we analyze the structural properties of the solvation water in antifreeze proteins (AFPs). The results of molecular dynamics analysis with the use of various parameters related to the structure of solvation water on the protein surface are presented. We found that in the vicinity of the active region responsible for the binding of AFPs to ice, the equilibrium is clearly shifted toward the formation of “ice-like aggregates,” and the solvation water has a more ordered ice-like structure. We have demonstrated that a reduction in the tendency to create “ice-like aggregates” results in a significant reduction in the antifreeze activity of the protein. We conclude that shifting the equilibrium in favor of the formation of “ice-like aggregates” in the solvation water in the active region is a prerequisite for the biological functionality of AFPs, at least for AFPs having a well-defined ice binding area. In addition, our results fully confirm the validity of the “anchored clathrate water” concept, formulated by Garnham et al. [Proc. Natl. Acad. Sci. U. S. A. 108, 7363 (2011)]." @default.
- W4386150907 created "2023-08-26" @default.
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- W4386150907 date "2023-08-25" @default.
- W4386150907 modified "2023-10-17" @default.
- W4386150907 title "Mechanism of antifreeze protein functioning and the “anchored clathrate water” concept" @default.
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- W4386150907 doi "https://doi.org/10.1063/5.0158590" @default.
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