折叠蛋白质的稳定性如何取决于界面水性质和残基-残基相互作用
How the stability of a folded protein depends on interfacial water properties and residue-residue interactions
摘要：
蛋白质只有在其天然状态下折叠时才起作用，但温度T和压力P的变化会诱导其解折叠。因此，对于每种蛋白质，在T-P热力学平面中存在稳定区（SR），在该稳定区之外生物分子变性。已知SR的延伸和形状取决于i）氨基酸序列天然状态下的特定蛋白质残基-残基相互作用和ii）水合界面处的水性质。在这里，我们通过蒙特卡罗模拟分析了不同的粗粒度蛋白质模型在显式水中的i）和ii）的变化如何影响SR。我们表明，溶剂性质ii）是必不可少的，以合理化SR形状在低T和高P，我们的发现是强大的参数变化和不同的蛋白质模型。这些结果可以帮助开发新的策略，设计新的合成生物聚合物。
英文摘要：
Proteins work only if folded in their native state, but changes in temperature T and pressure P induce their unfolding. Therefore for each protein there is a stability region (SR) in the T-P thermodynamic plane outside which the biomolecule is denaturated. It is known that the extension and shape of the SR depend on i) the specific protein residue-residue interactions in the native state of the amino acids sequence and ii) the water properties at the hydration interface. Here we analyze by Monte Carlo simulations of different coarse-grained protein models in explicit water how changes in i) and ii) affect the SR. We show that the solvent properties ii) are essential to rationalize the SR shape at low T and high P and that our finding are robust with respect to parameter changes and with respect to different protein models. These results can help in developing new strategies for the design of novel synthetic biopolymers.
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