Abstract
Significant advances have been made in understanding the basic thermodynamic principles that govern protein salting out and stabilization by solvent components. A rule has been established that preferential exclusion of a compound must lead to salting out, whereas stabilization depends on a fine interplay between exclusion from and binding to the native and unfolded proteins. A physico-chemical basis has been provided for the selection of osmolytes by nature, and the basis of structure stabilization by salts has been established for halophiles. A rigorous thermodynamic analysis has identified the basic difference between site occupancy and preferential interactions, showing that it is the latter that control stabilization or denaturation.
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