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首页> 外文期刊>The Journal of Chemical Physics >The opposing effects of isotropic and anisotropic attraction on association kinetics of proteins and colloids
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The opposing effects of isotropic and anisotropic attraction on association kinetics of proteins and colloids

机译：各向同性和各向异性吸引对蛋白质和胶体关联动力学的反对作用

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摘要

The association and dissociation of particles via specific anisotropic interactions is a fundamental process, both in biology (proteins) and in soft matter (colloidal patchy particles). The presence of alternative binding sites can lead to multiple productive states and also to non-productive "decoy" or intermediate states. Besides anisotropic interactions, particles can experience non-specific isotropic interactions. We employ single replica transition interface sampling to investigate how adding a non-productive binding site or a nonspecific isotropic interaction alters the dimerization kinetics of a generic patchy particle model. The addition of a decoy binding site reduces the association rate constant, independent of the site's position, while adding an isotropic interaction increases it due to an increased rebinding probability. Surprisingly, the association kinetics becomes non-monotonic for a tetramer complex formed by multivalent patchy particles. While seemingly identical to two-particle binding with a decoy state, the cooperativity of binding multiple particles leads to a kinetic optimum. Our results are relevant for the understanding and modeling of biochemical networks and self-assembly processes. Published by AIP Publishing.
机译：通过特异性各向异性相互作用的颗粒的关联和解离是生物学（蛋白质）和软质（胶体斑块颗粒）的基本过程。替代结合位点的存在可以导致多种生产性状态，也可以导致非生产的“诱饵”或中间状态。除各向异性相互作用外，颗粒还可以体验非特异性各向同性相互作用。我们采用单副产转变界面采样来研究添加非生产结合位点或非特异性各向同性相互作用改变了通用斑块粒子模型的二聚化动力学。添加诱饵结合位点减少了与位点的位置无关的关联速率常数，同时添加各向同性相互作用，由于螺纹概率增加，增加它。令人惊讶的是，缔合动力学成为由多价蛋白颗粒形成的四聚体复合物的非单调。虽然看似与诱饵状态的双粒子结合相同，但是结合多个颗粒的合作率导致动力学最佳。我们的结果与生化网络和自组装过程的理解和建模有关。通过AIP发布发布。

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