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- W2009003235 abstract "The effects of Li+ and H3O+ on the conformation of bovine serum albumin in aqueous solutions at room temperature are compared. At low pH (high concentration of H3O+) the change in conformation of the protein is demonstrated by an increase in effective volume, a decrease in helical content and a blue shift of tyrosyl residue. A similar change is observed for the protein in highly concentrated LiCl solution (6.0–7.0 M) at neutral pH. However, the H3O+ is 12,000 times more powerful than the Li+ in destabilizing the protein molecule. This is consistent with their thermodynamic and kinetic properties, since the H3O+ is often different from the Li+ in several orders of magnitude. While the changes in structural properties of the protein are almost identical in both the acidic solution and the highly concentrated LiCl solution, further study using dioxane as a probe suggests different mechanisms under which the changes occur. The effect of H3O+ is related to electrostatic force, whereas the effect of Li+ is related to both the electrostatic and hydrophobic forces. These two major forces are believed to be responsible for the conformation of protein molecules." @default.
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- W2009003235 date "2009-01-12" @default.
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- W2009003235 title "BOVINE SERUM ALBUMIN IN LITHIUM CHLORIDE SOLUTIONS. III. A Comparative Study of Li+ and H3O+ Effects" @default.
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- W2009003235 doi "https://doi.org/10.1111/j.1399-3011.1975.tb02419.x" @default.
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