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 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.

当蛋白质的水合壳充满每克蛋白质至少 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显着的反相关。这意味着低势能、水合良好的蛋白质构象异构体往往比高能异构体更坚硬。另一方面，在 CASP 目标 624 的情况下，当其水合壳被填充时，在晶体结构和预测实验中提出的最佳构象异构体之间观察到显着的能隙，强烈表明包含明确的水分子可能有助于识别在好看的人中不太可能符合条件。