ELECTRO STATIC OF ALPHA & BETA BARREL PROTEINS

静电阿尔法

• 批准号: 6309534
• 负责人: Daniel Roberto Ripoll
• 金额: $ 2.43万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-12-01 至 2000-11-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6309534
• 关键词: biological products; biomedical resource; computers; enzymes; structural biology; technology /technique

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.

研究了α/β桶酶的静电性质 通过检查包含该折叠的六种酶的结构： 磷酸丙糖异构酶，果糖-1，6-二磷酸醛缩酶， 丙酮酸激酶，扁桃酸消旋酶，三甲胺脱氢酶， 乙醇酸氧化酶和narbonin，一种具有这种折叠的蛋白质， 没有任何已知的酶活性。 的中坚力量 α/β-桶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 当侧链包含在所述聚合物中时， 计算，观察到的骨架的静电图案是 整体守恒和单位电场线数 表面增加。 本文计算的静电场 与已知的该酶家族对 带负电荷的基质。 计算是在 使用DelPhi程序。