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- W2000925202 abstract "Recently, we have elaborated a thermodynamical theory that could coherently interpret the apparently diverse effects of Hofmeister ions on proteins, based on a single physical parameter, the protein-water interfacial tension (Dér et al., Journal of Physical Chemistry B. 2007, 111, 5344-5350). This theory, implying a sort of liquid drop model, predicts changes in protein conformational fluctuations upon addition of Hofmeister salts (containing either kosmotropic or chaotropic anions) to the medium. Despite the success of the theory in describing the diversity of Hofmeister phenomena, a direct evidence for salt-induced changes of protein-water interfacial tension correlated with the Hofmeister series has been still missing, because of technical difficulties. In the framework of the present study, we addressed this point by a molecular dynamics (MD) approach. MD calculations on the temperature-induced unfolding of Tryptophan cage miniprotein were performed, using explicit water molecules to model the surroundings of the protein. Changes of the protein structure and dynamics upon increasing the ambient temperature were monitored in the presence and absence of typical kosmotropic and chaotropic salts. It was established that salt ions change the level of conformational fluctuations of the miniprotein according to their position in the Hofmeister series. From equlibrium fluctuations of the solvent accessible surface area of the protein, the mean value of protein-water interfacial tension was determined. The results present a strong evidence for the central role of fluctuations and solute-water interfacial tension in protein-related Hofmeister phenomena." @default.
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- W2000925202 date "2014-01-01" @default.
- W2000925202 modified "2023-09-30" @default.
- W2000925202 title "Protein-Water Interfacial Tension Drives Hofmeister Effects" @default.
- W2000925202 doi "https://doi.org/10.1016/j.bpj.2013.11.3676" @default.
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