COMPUTATION OF THE ELECTROPHORETIC MOBILITY OF PROTEINS
COMPUTATION OF THE ELECTROPHORETIC MOBILITY OF PROTEINS
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DOI：
10.1016/s0006-3495(95)80286-9
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发表时间：
1995-03-01
影响因子：
3.4
通讯作者：
LENHOFF, AM
中科院分区：
文献类型：
--
作者：
CHAE, KS;LENHOFF, AM
提出了一种计算蛋白质在自由溶液中的电泳迁移率的方案，考虑了蛋白质形状和电荷分布的细节。Teubner的方法使用边界积分公式来实现，在该边界积分公式中，使用边界元法数值求解由于所施加的场而引起的速度分布、分子周围的平衡电势和电势分布。数值结果与相应的亨利分析的半解析特化结果在球面上吻合得很好。对于蛋白质系统，该方法适用于溶菌酶和核糖核酸酶A。在这两种情况下，预测的迁移率张量是相当各向同性的，所得到的标量迁移率显着小于相等体积和净电荷的球体。与先前发表的核糖核酸酶的实验结果的比较表明，协议是优秀的存在下的净电荷，但较差的零电荷点。该方法可能是有用的评估近似方法估计蛋白质电泳迁移率和使用电泳测量，以获得洞察蛋白质上的电荷分布。
A scheme is presented for computing the electrophoretic mobility of proteins in free solution, accounting for the details of the protein shape and charge distribution. The method of Teubner is implemented using a boundary integral formulation within which the velocity distribution, the equilibrium electrical potential around the molecule, and the potential distribution due to the applied field are solved for numerically using the boundary element method. Good agreement of the numerical result is obtained for spheres with the corresponding semi-analytical specialization of Henry's analysis. For protein systems, the method is applied to lysozyme and ribonuclease A. In both cases, the predicted mobility tensors are fairly isotropic, with the resulting scalar mobilities being significantly smaller than for spheres of equal volume and net charge. Comparisons with previously published experimental results for ribonuclease show agreement to be excellent in the presence of a net charge, but poorer at the point of zero charge. The approach may be useful for evaluating approximate methods for estimating protein electrophoretic mobilities and for using electrophoretic measurements to obtain insight into charge distributions on proteins.