Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies
Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies
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DOI：
10.1590/s0100-879x2005000800003
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发表时间：
2005-08-01
影响因子：
2.3
通讯作者：
Royer, C.A.
中科院分区：
文献类型：
--
作者：
Royer, C.A.
对蛋白质结构和稳定性的透彻理解要求我们阐明温度和压力对蛋白质构象转变的影响的分子基础。虽然温度的影响是相对较好的理解和热容量的变化时，展开已经合理地很好的参数化，了解压力的影响的状态是不够先进。最终，伴随蛋白质构象转变的体积变化（在压力效应的基础上）的定量参数化将是必需的。本报告介绍了一个定性假设的基础上，现有的模型化合物数据的分子基础上的体积变化后，蛋白质展开及其对温度的依赖性。
A thorough understanding of protein structure and stability requires that we elucidate the molecular basis for the effects of both temperature and pressure on protein conformational transitions. While temperature effects are relatively well understood and the change in heat capacity upon unfolding has been reasonably well parameterized, the state of understanding of pressure effects is much less advanced. Ultimately, a quantitative parameterization of the volume changes (at the basis of pressure effects) accompanying protein conformational transitions will be required. The present report introduces a qualitative hypothesis based on available model compound data for the molecular basis of volume change upon protein unfolding and its dependence on temperature.