Impact of Protein Denaturants and Stabilizers on Water Structure

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• 作者：Joseph D. Batchelor ; Alina Olteanu ; Ashutosh Tripathy ; and Gary J. Pielak
• 刊名：Journal of the American Chemical Society
• 出版年：2004
• 出版时间：February 25, 2004
• 年：2004
• 卷：126
• 期：7
• 页码：1958 - 1961
• 全文大小：69K
• 年卷期：v.126,no.7(February 25, 2004)
• ISSN：1520-5126

文摘

It is of great interest to determine how solutes such as urea, sugars, guanidinium salts, andtrimethylamine N-oxide affect the stability, solubility, and solvation of globular proteins. A key hypothesisin this field states that solutes affect protein stability indirectly by making or breaking water structure. Weused a new technique, pressure perturbation calorimetry, to measure the temperature dependence of asolute's partial compressibility. Using fundamental thermodynamic relations, we converted these data tothe pressure dependence of the partial heat capacity to examine the impact of protein stabilizing anddenaturing solutes on water structure by applying the classic two-state mixture model for water. Contraryto widely held expectations, we found no correlation between a solute's impact on water structure and itseffect on protein stability. Our results indicate that efforts to explain solute effects should focus on otherhypotheses, including those based on preferential interaction and excluded volume.