Contini A, Tiana G
Department of Physics, Università degli Studi di Milano, via Celoria 16, 20133 Milano, Italy.
Department of Physics, Università degli Studi di Milano, and INFN, via Celoria 16, 20133 Milano, Italy.
J Chem Phys. 2015 Jul 14;143(2):025103. doi: 10.1063/1.4926665.
The study of correlated mutations in alignments of homologous proteins proved to be successful not only in the prediction of their native conformation but also in the development of a two-body effective potential between pairs of amino acids. In the present work, we extend the effective potential, introducing a many-body term based on the same theoretical framework, making use of a principle of maximum entropy. The extended potential performs better than the two-body one in predicting the energetic effect of 308 mutations in 14 proteins (including membrane proteins). The average value of the parameters of the many-body term correlates with the degree of hydrophobicity of the corresponding residues, suggesting that this term partly reflects the effect of the solvent.
对同源蛋白质比对中的相关突变进行研究，结果证明不仅在预测其天然构象方面很成功，而且在开发氨基酸对之间的两体有效势方面也很成功。在本工作中，我们扩展了有效势，基于相同的理论框架引入了一个多体项，利用最大熵原理。在预测14种蛋白质（包括膜蛋白）中308个突变的能量效应时，扩展势比两体势表现更好。多体项参数的平均值与相应残基的疏水性程度相关，这表明该项部分反映了溶剂的影响。
