POLAR HYDROGEN POSITIONS IN PROTEINS - EMPIRICAL ENERGY PLACEMENT AND NEUTRON-DIFFRACTION COMPARISON
POLAR HYDROGEN POSITIONS IN PROTEINS - EMPIRICAL ENERGY PLACEMENT AND NEUTRON-DIFFRACTION COMPARISON
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DOI：
10.1002/prot.340040208
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发表时间：
1988-01-01
期刊：
影响因子：
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通讯作者：
KARPLUS, M
中科院分区：
文献类型：
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作者：
BRUNGER, AT;KARPLUS, M
提出了一种预测蛋白质中氢位置的方法。该方法基于重原子位置的知识，例如从X射线晶体学中获得的。它采用的能量最小化限于氢原子与普通重原子或单个水分子结合的环境。该方法不限于蛋白质，并且可以不经修饰地应用于非极性氢和核酸。该方法已应用于胰蛋白酶核糖核酸酶A和牛胰蛋白酶抑制剂的中子衍射结构。构造和观察到的氢的位置的比较显示，除了在几个能量相似的构象是可能的情况下，很少的偏差。对赖氨酸氨基和丝氨酸、苏氨酸、酪氨酸羟基的旋转势能的分析表明，在晶体和构建的结构中，最低固有扭转能的构象在统计上是有利的。
A method for the prediction of hydrogen positions in proteins is presented. The method is based on the knowledge of the heavy atom positions obtained, for instance, from X‐ray crystallography. It employs an energy minimization limited to the environment of the hydrogen atoms bound to a common heavy atom or to a single water molecule. The method is not restricted to proteins and can be applied without modification to nonpolar hydrogens and to nucleic acids. The method has been applied to the neutron diffraction structures of trypsin ribonuclease A, and bovine pancreatic trypsin inhibitor. A comparison of the constructed and the observed hydrogen positions shows few deviations except in situations in which several energetically similar conformations are possible. Analysis of the potential energy of rotation of Lys amino and Ser, Thr, Tyr hydroxyl groups reveals that the conformations of lowest intrinsic torsion energies are statistically favored in both the crystal and the constructed structures.