Eisenhaber F
Institut für Biochemie der Charité, Medizinische Fakultät, Humboldt-Universität zu Berlin, Berlin-Mitte, Germany.
Protein Sci. 1996 Aug;5(8):1676-86. doi: 10.1002/pro.5560050821.
For the first time, a direct approach for the derivation of an atomic solvation parameter from macromolecular structural data alone is presented. The specific free energy of solvation for hydrophobic surface regions of proteins is delineated from the area distribution of hydrophobic surface patches. The resulting value is 18 cal/(mol.A2), with a statistical uncertainty of +/-2 cal/mol.A2) at the 5% significance level. It compares favorably with the parameters for carbon obtained by other authors who use the the crystal geometry of succinic acid or energies of transfer from hydrophobic solvent to water for small organic compounds. Thus, the transferability of atomic solvation parameters for hydrophobic atoms to macromolecules has been directly demonstrated. A careful statistical analysis demonstrates that surface energy parameters derived from thermodynamic data of protein mutation experiments are clearly less confident.
首次提出了一种仅从大分子结构数据推导原子溶剂化参数的直接方法。根据疏水表面斑块的面积分布，描绘了蛋白质疏水表面区域的溶剂化比自由能。得到的值为18 cal/(mol·Å²)，在5%显著水平下的统计不确定度为±2 cal/(mol·Å²)。它与其他作者通过琥珀酸晶体几何结构或从小有机化合物从疏水溶剂转移到水的能量获得的碳参数相比具有优势。因此，已直接证明了疏水原子的原子溶剂化参数对大分子的转移性。仔细的统计分析表明，从蛋白质突变实验的热力学数据得出的表面能参数明显缺乏可信度。
