Banach Mateusz, Roterman Irena
Department of Bioinformatics and Telemedicine, Collegium Medium - Jagiellonian University, Lazarza 16, 31-530 Krakow, Poland.
Bioinformation. 2009 Sep 30;4(3):98-100. doi: 10.6026/97320630004098.
The identification of the surface area able to generate the protein-protein complexation ligand and ion ligation is critical for the recognition of the biological function of particular proteins. The technique based on the analysis of the irregularity of hydrophobicity distribution is used as the criterion for the recognition of the interaction regions. Particularly, the exposure of hydrophobic residues on the surface of protein as well as the localization of the hydrophilic residues in the hydrophobic core is treated as potential area ready to interact with external molecules. The model based on the "fuzzy oil drop" approach treating the protein molecule as the drop of hydrophobicity concentrated in the central part of structure with the hydrophobicity close to zero on the surface according to 3-dimensional Gauss function. The comparison with the observed hydrophobicy in particular protein reveals some irregularities. These irregularities seem to represent the aim-oriented localization.
确定能够产生蛋白质 - 蛋白质络合配体和离子连接的表面积对于识别特定蛋白质的生物学功能至关重要。基于疏水性分布不规则性分析的技术被用作识别相互作用区域的标准。特别是，蛋白质表面疏水残基的暴露以及亲水残基在疏水核心中的定位被视为可能与外部分子相互作用的潜在区域。基于“模糊油滴”方法的模型将蛋白质分子视为疏水性集中在结构中心部分的液滴，根据三维高斯函数，其表面疏水性接近零。与特定蛋白质中观察到的疏水性进行比较揭示了一些不规则性。这些不规则性似乎代表了目标导向的定位。
