Protein stability; optimization of electrostatic contributions by partially neutralizing surface ionic charges
Protein stability; optimization of electrostatic contributions by partially neutralizing surface ionic charges
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DOI：
10.1016/s0303-2647(97)00043-9
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发表时间：
1997-01-01
期刊：
影响因子：
1.6
通讯作者：
Soda, K
中科院分区：
文献类型：
--
作者：
Miki, Y;Kakuyama, K;Soda, K
“部分电荷中和法”是为了研究蛋白质中正电荷和负电荷的相对数量对其结构稳定性的影响而开发的。给定数量的带正电或带负电的基团在其所有可能的组合中被中和，以生成一整套不同的物种。通过数值求解水溶液的泊松-玻尔兹曼方程来计算每种物质的库仑能量。在中性 pH 条件下，采用 Debye-Huckel 筛选参数 kappa = 1 nm(-1) 部分中和水溶液中金枪鱼细胞色素 c 的赖氨酸残基，可以很好地定性再现在 pH 7 的物理化学测量中观察到的乙酰化细胞色素 c 的不稳定。还用本方法研究了 pH 2 下其熔球状态的稳定性。研究表明，静电对天然蛋白质结构稳定性的贡献可以通过改变其正电荷和负电荷数量的差异来优化。 (C) 1997 爱思唯尔科学爱尔兰有限公司
'Partial Charge-Neutralization Method' is developed to study influence of the relative amount of positive and negative charges in proteins on their structural stability. A given number of either positively or negatively charged groups are neutralized in all of their possible combinations to generate a whole set of distinct species. The Coulomb energy of each species is calculated by numerically solving the Poisson-Boltzmann equation for aqueous solutions. Partial neutralization of lysine residues of tuna cytochrome c in aqueous solution at neutral pH with the Debye-Huckel screening parameter kappa = 1 nm(-1) reproduces qualitatively well the destabilization of acetylated cytochrome c observed in physicochemical measurements at pH 7. The stabilization of its molten globule state at pH 2 is also studied with the present method. It is shown that the electrostatic contribution to the structural stability of natural proteins can be optimized by changing the difference in number of their positive and negative charges. (C) 1997 Elsevier Science Ireland Ltd.