Vendruscolo M
Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, Oxford, OX1 3QT UK.
J Biol Phys. 2001 Jun;27(2-3):205-15. doi: 10.1023/A:1013152026788.
We propose a simple criterion based on the Z-scoreto assess the quality of energy functions for protein folding: one should obtain Z>-10 for the equilibrium ensembleat about native conditions. We derive this criterionby studying a Go model with random errors added to the native interactions. The dependence of the Z-score on the thermodynamic parameters,including the noise, can be precisely obtained in this case,as the ground state of the model is known exactly.We apply this criterion to rapidly rule out two otherwise promisingpairwise energy approximations.The advantage of adopting the present criterionis that it is not necessary to know the ground state of an energy function to assess its quality. It is sufficient to compute the Z-scorefrom a single equilibrium simulation at around the folding temperature.
我们提出了一种基于Z分数的简单标准,用于评估蛋白质折叠能量函数的质量:在接近天然条件下的平衡系综中,Z值应大于 -10。我们通过研究在天然相互作用中添加随机误差的Go模型得出了这个标准。在这种情况下,由于模型的基态是精确已知的,所以可以精确得到Z分数对包括噪声在内的热力学参数的依赖性。我们应用这个标准迅速排除了另外两个有前景的成对能量近似。采用本标准的优点是,评估能量函数的质量时无需知道其基态。在折叠温度附近通过单次平衡模拟计算Z分数就足够了。