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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Weak Self-Interactions of Globular Proteins Studied by Small-Angle X-ray Scattering and Structure-Based Modeling
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Weak Self-Interactions of Globular Proteins Studied by Small-Angle X-ray Scattering and Structure-Based Modeling

机译：小角X射线散射和基于结构的模型研究的球蛋白的弱自我相互作用

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摘要

We investigate protein—protein interactions in solution by small-angle X-ray scattering (SAXS) and theoretical modeling. The structure factor for solutions of bovine pancreatic trypsin inhibitor (BPTI), myoglobin (Mb), and intestinal fatty acid-binding protein (IFABP) is determined from SAXS measurements at multiple concentrations, from Monte Carlo simulations with a coarse-grained structure-based interaction model, and from analytic approximate solutions of two idealized colloidal interaction models without adjustable parameters. By combining these approaches, we find that the structure factor is essentially determined by hard-core and screened electrostatic interactions. Other soft short-ranged interactions (van der Waals and solvation-related) are either individually insignificant or tend to cancel out. The structure factor is also not significantly affected by charge fluctuations. For Mb and IFABP, with a small net charge and relatively symmetric charge distribution, the structure factor is well described by a hard-sphere model. For BPTI, with a larger net charge, screened electrostatic repulsion is also important, but the asymmetry of the charge distribution reduces the repulsion from that predicted by a charged hard-sphere model with the same net charge. Such charge asymmetry may also amplify the effect of shape asymmetry on the protein—protein potential of mean force.
机译：我们通过小角度X射线散射（SAXS）和理论模型研究溶液中的蛋白质-蛋白质相互作用。牛胰胰蛋白酶抑制剂（BPTI），肌红蛋白（Mb）和肠脂肪酸结合蛋白（IFABP）溶液的结构因子是根据多种浓度下的SAXS测量，蒙特卡罗模拟和基于粗粒度结构的方法确定的相互作用模型，以及两个没有可调参数的理想胶体相互作用模型的解析近似解。通过组合这些方法，我们发现结构因子主要由硬核和屏蔽的静电相互作用决定。其他柔和的短程相互作用（范德华和与溶剂化有关）则微不足道或趋于抵消。电荷波动也不会显着影响结构因子。对于Mb和IFABP，具有小的净电荷和相对对称的电荷分布，其结构因子可以通过硬球模型很好地描述。对于具有较大净电荷的BPTI，屏蔽的静电排斥也很重要，但是电荷分布的不对称性会减少具有相同净电荷的带电硬球模型所预测的排斥。这种电荷不对称性也可能会放大形状不对称性对蛋白质（平均力的蛋白质电位）的影响。

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