Predicting the energetics of osmolyte-induced protein folding/unfolding
Predicting the energetics of osmolyte-induced protein folding/unfolding
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DOI：
10.1073/pnas.0507053102
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发表时间：
2005-10-18
影响因子：
11.1
通讯作者：
Bolen, DW
中科院分区：
文献类型：
--
作者：
Auton, M;Bolen, DW
蛋白质生物化学中的主要热力学目标是获得对负责折叠/展开的详细能量变化的预测性理解。通过使用最近确定的侧链和骨干转移的自由能从水渗透和Tanford的转移模型，我们证明了长期寻求的目标预测溶剂依赖性的合作蛋白质折叠/展开自由能的变化（m值）可以实现。此外，该方法允许将折叠/展开自由能变化分解为来自肽骨架和残基侧链的单独贡献。
A primary thermodynamic goal in protein biochemistry is to attain predictive understanding of the detailed energetic changes that are responsible for folding/unfolding. Through use of recently determined free energies of side-chain and backbone transfer from water to osmolytes and Tanford's transfer model, we demonstrate that the long-sought goal of predicting solvent-dependent cooperative protein folding/unfolding free-energy changes (m values) can be achieved. Moreover, the approach permits dissection of the folding/unfolding free-energy changes into individual contributions from the peptide backbone and residue side chains.