Electrostatic contributions to heat capacity changes of DNA-ligand binding
Electrostatic contributions to heat capacity changes of DNA-ligand binding
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DOI：
10.1016/s0006-3495(98)77566-6
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发表时间：
1998-08-01
影响因子：
3.4
通讯作者：
Sharp, K
中科院分区：
文献类型：
--
作者：
Gallagher, K;Sharp, K
显着的热容量变化（Δ C-p）往往伴随着蛋白质解折叠，蛋白质结合，和特定的DNA-配体结合反应。这种变化被广泛用于分析疏水性和极性水合作用所产生的贡献。目前的模型将Δ C-p的大小与分子的溶剂可及表面积（阿萨）相关联。然而，对于许多结合系统，特别是那些涉及非肽配体，这些模型预测的Δ C-p是显着不同的实验测量值。静电相互作用提供了一个潜在的源的热容量的变化，并不与阿萨的规模，使用有限差分泊松-玻尔兹曼方法（FDPB），我们已经确定了静电的贡献与DNA结合反应，涉及配体DAPI，netropsin，lexitropsin，和λ阻遏物结合结构域的结合相关的Δ C-p。
Significant heat capacity changes (Delta C-p) often accompany protein unfolding, protein binding, and specific DNA-ligand binding reactions. Such changes are widely used to analyze contributions arising from hydrophobic and polar hydration. Current models relate the magnitude of Delta C-p to the solvent accessible surface area (ASA) of the molecule. However, for many binding systems-particularly those involving non-peptide ligands-these models predict a Delta C-p that is significantly different from the experimentally measured value. Electrostatic interactions provide a potential source of heat capacity changes and do not scale with ASA, Using finite-difference Poisson-Boltzmann methods (FDPB), we have determined the contribution of electrostatics to the Delta C-p associated with binding for DNA binding reactions involving the ligands DAPI, netropsin, lexitropsin, and the lambda repressor binding domain.