论文标题
在水合蛋白的振动自由能上
On the vibrational free energy of hydrated proteins
论文作者
论文摘要
当蛋白质的水合壳每克每克蛋白质至少填充0.6克水时，观察到振动自由能与能量最小化构象异构体的势能之间存在明显的抗相关性。这意味着低势能（水分良好，蛋白质构象体）往往比高能量更刚性。另一方面，在CASP目标624的情况下，当填充水合壳时，在预测实验期间提出的晶体结构和提出的最佳构象体之间会观察到显着的平均能量差距，这强烈表明，包括明确的水分子可能有助于识别好看起来好看的构型。
When the hydration shell of a protein is filled with at least 0.6 gram of water per gram of protein, a significant anti-correlation between the vibrational free energy and the potential energy of energy-minimized conformers is observed. This means that low potential energy, well-hydrated, protein conformers tend to be more rigid than high-energy ones. On the other hand, in the case of CASP target 624, when its hydration shell is filled, a significant average energy gap is observed between the crystal structure and the best conformers proposed during the prediction experiment, strongly suggesting that including explicit water molecules may help identifying unlikely conformers among good-looking ones.
