ELECTRO STATIC OF ALPHA & BETA BARREL PROTEINS

研究了α/β-桶酶的静电性质。 通过研究包含该折叠的六种酶的结构： 磷酸三糖异构酶、果糖-1，6-生物磷酸醛缩酶、 丙酮酸激酶，扁桃酸消旋酶，三甲胺脱氢酶， 乙醇酸氧化酶和纳波宁，一种具有这个折叠的蛋白质，但 没有任何已知的酶活性。中国社会的中坚力量 Alpha/Beta-Barrel具有明显的静电场模式， 对酶(蛋白质)的总体贡献很大 静电指纹。当侧链包含在 计算，观察到的主干的静电模式是 全局守恒和单位电场线的数量 曲面增加。本工作中计算的静电场 与这个酶家族的已知偏好是一致的 带负电荷的衬底。这些计算是进行的 使用Delphi程序。

Electrostatic properties of alpha/beta-barrel enzymes were studied by examining the structures of six enzymes containing this fold: triose phosphate isomerase, fructose-1,6-biophosphate aldolase, pyruvate kinase, mandelate racemase, trimethylamine dehydrogenase, glycolate oxidase and of narbonin, a protein with this fold but without any known enzymatic activity. The backbone of the alpha/beta-barrel has a distinct electrostatic field pattern, which contributes substantially to the enzyme's (protein) overall electrostatic fingerprints. When the side-chains are included in the calculations, the electrostatic pattern observed for the backbone is globally conserved and the number of electric field lines per unit surface increases. The electrostatic field calculated in this work are consistent with the known preference of this family of enzymes for negatively charged substrates. The calculations were carried out using the program DelPhi.