A theory of protein-resin interaction in hydrophobic interaction chromatography.
A theory of protein-resin interaction in hydrophobic interaction chromatography.
复制标题
疏水相互作用色谱中蛋白质-树脂相互作用的理论。
DOI：
10.1016/j.chroma.2005.01.016
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
J. Asenjo
中科院分区：
文献类型：
--
作者：
A. Mahn;G. Zapata;J. Asenjo
使用 AutoDock 3.0 程序进行对接模拟，以研究几种核糖核酸酶之间相互作用的表面积和 Phenyl Sepharose™ 中使用的疏水部分的简化模型。对于每种核糖核酸酶，对由 100 个随机结构组成的群体进行了 80 次独立模拟，并从中获得了最可能的对接蛋白质配体构象。基于定性和定量的考虑，使用了一种新的方法来选择最可能的构象。确定了每种蛋白质中相互作用的氨基酸。测定界面区的平均表面疏水性（局部疏水性，LH）。 LH 显示出与不同核糖核酸酶实验确定的“疏水接触面积”(HCA) 以及无量纲保留时间 (r2=0.90) 的高度相关性 (r2=0.99)。这项研究使我们能够识别蛋白质表面上最有可能参与 HIC 中蛋白质保留的区域，而无需进行繁琐的实验工作。鉴于获得的良好相关性水平，这种新方法可能构成一种可用于预测 HIC 中蛋白质行为的新方法。
Docking simulations were performed in order to investigate surface area of interaction between several ribonucleases and a reduced model for the hydrophobic moiety used in Phenyl Sepharose™ using the program AutoDock 3.0. For each ribonucelase, 80 independent simulations with populations consisting of 100 random structures were performed and from these the most probable docked protein–ligand conformations were obtained. A new methodology was used to select the most probable conformations, based on qualitative and quantitative considerations. The interacting amino acids in each protein were identified. The average surface hydrophobicity of the interfacial zone (local hydrophobicity, LH) was determined. The LH showed a high correlation level (r2=0.99) with the “hydrophobic contact area” (HCA) experimentally determined for the different ribonucleases as well as with the dimensionless retention time (r2=0.90). This study allowed us to identify the zones on the protein surface most probably involved in protein retention in HIC, without tedious experimental work. Given the good correlation level obtained, this new methodology may constitute a novel approach that could be used to predict protein behavior in HIC.
影响因子：
5.5
作者：
MIYAZAWA, S;JERNIGAN, RL
通讯作者：
JERNIGAN, RL