CALCULATION OF THE ELECTRIC-POTENTIAL IN THE ACTIVE-SITE CLEFT DUE TO ALPHA-HELIX DIPOLES
CALCULATION OF THE ELECTRIC-POTENTIAL IN THE ACTIVE-SITE CLEFT DUE TO ALPHA-HELIX DIPOLES
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DOI：
10.1016/0022-2836(82)90505-8
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发表时间：
1982-01-01
影响因子：
5.6
通讯作者：
WATSON, HC
中科院分区：
文献类型：
--
作者：
WARWICKER, J;WATSON, HC
采用宏观介电模型建立了蛋白质-溶剂体系的静电方程。应用数值解法，能够计算由于蛋白质内的电荷而导致的蛋白质外部的电势。糖酵解酶[酵母]磷酸甘油酸酯是一种α/。β的蛋白质结合带负电荷的底物，进行了研究。对具有正电荷和负电荷的螺旋偶极进行建模表明，α-螺旋结构可以稳定负电荷底物在活性位点裂缝的酶的能量为几个kT。
A macroscopic dielectric model was used to set up the electrostatic equation for the protein-solvent system. A numerical method of solution was applied, enabling calculation of the electric potential outside a protein due to the charges within the protein. The glycolytic enzyme [yeast] phosphoglycerate mutase, which is an .alpha./.beta. protein binding negatively charged substrates, was studied. Modelling the helix dipoles with positive and negative charges shows that the .alpha.-helical structure could stabilize negatively charged substrates in the active site cleft of an enzyme with an energy of a few kT.