STABILIZATION OF PROTEIN-STRUCTURE BY SUGARS
STABILIZATION OF PROTEIN-STRUCTURE BY SUGARS
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DOI：
10.1021/bi00268a033
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发表时间：
1982-01-01
期刊：
影响因子：
2.9
通讯作者：
TIMASHEFF, SN
中科院分区：
文献类型：
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作者：
ARAKAWA, T;TIMASHEFF, SN
用高精度密度计测定了乳糖和葡萄糖水溶液体系中蛋白质与溶剂组分的优先相互作用。在所有情况下，蛋白质优先水合;即，将这些糖添加到蛋白质的水溶液中导致不利的自由能变化。这种效果随着蛋白质表面积的增加而增加，解释了这些糖的蛋白质稳定作用及其对蛋白质缔合的增强作用。优先相互作用参数与糖对水表面张力的影响的相关性，即，它们的正表面张力增量，导致糖的表面自由能扰动在它们与蛋白质的优先相互作用中起主导作用的结论。其他影响因素是糖的排阻体积和蛋白质表面的化学性质。
The preferential interaction of proteins with solvent components was measured in aqueous lactose and glucose systems by using a high precision densimeter. In all cases, the protein was preferentially hydrated; i.e., addition of these sugars to an aqueous solution of the protein resulted in an unfavorable free-energy change. This effect increased with an increase in protein surface area, explaining the protein stabilizing action of these sugars and their enhancing effect of protein associations. Correlation of the preferential interaction parameter with the effect of the sugars on the surface tension of water, i.e., their positive surface tension increment, led to the conclusion that the surface free energy perturbation by sugars plays a predominant role in their preferential interaction with proteins. Other contributing factors are the exclusion volume of the sugars and the chemical nature of the protein surface.