Protein folding, stability, and solvation structure in osmolyte solutions
Protein folding, stability, and solvation structure in osmolyte solutions
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DOI：
10.1529/biophysj.105.067330
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发表时间：
2005-11-01
影响因子：
3.4
通讯作者：
Bolen, DW
中科院分区：
文献类型：
--
作者：
Rösgen, J;Pettitt, BM;Bolen, DW
了解细胞质中拥挤条件对其生物分子的影响对生物化学、医学和制药科学具有明显的重要性。我们之前使用小的生化化合物来拥挤蛋白质溶液的工作表明，对它们的非理想行为的定量描述是可能的和直接的。在这里，我们展示了非理想溶液行为的结构起源。我们通过对溶液中大分子相对于第三组分浓度的m值或自由能差变化的结构分析，讨论了这些发现对蛋白质折叠稳定性和拥挤溶液中溶剂化的影响。
An understanding of the impact of the crowded conditions in the cytoplasm on its biomolecules is of clear importance to biochemical, medical, and pharmaceutical science. Our previous work on the use of small biochemical compounds to crowd protein solutions indicates that a quantitative description of their nonideal behavior is possible and straightforward. Here, we show the structural origin of the nonideal solution behavior. We discuss the consequences of these findings regarding protein folding stability and solvation in crowded solutions through a structural analysis of the m-value or the change in free-energy difference of a macromolecule in solution with respect to the concentration of a third component.