结合和未结合蛋白质的相对扩散系数可以控制趋化方向性
The Relative Diffusivities of Bound and Unbound Protein Can Control Chemotactic Directionality
摘要：
基于酶的系统已经显示出响应于其底物梯度而进行定向运动。在这里，我们制定了一个动力学模型来分析响应于配体梯度的蛋白质分子系综的定向运动。已经进行了类似的分析，以探测酶分子在催化条件下响应于底物梯度的运动。在这两种情况下，当配体/底物结合的蛋白质的扩散率低于未结合的蛋白质的扩散率（正趋化性）时，预测配体/底物梯度的净移动。相反，当配体/底物结合的蛋白质的扩散率高于未结合的蛋白质的扩散率（负趋化性）时，预期配体/底物梯度向下移动。这项工作强调了测量结合蛋白的扩散率并将其与游离蛋白进行比较的至关重要性。
英文摘要：
Enzyme-based systems have been shown to undergo directional motion in response to their substrate gradient. Here, we formulate a kinetic model to analyze the directional movement of an ensemble of protein molecules in response to a gradient of the ligand. A similar analysis has been performed to probe the motion of enzyme molecules in response to a gradient of the substrate under catalytic conditions. In both cases, a net movement up the ligand/substrate gradient is predicted when the diffusivity of the ligand/substrate-bound protein is lower than that of the unbound protein (positive chemotaxis). Conversely, movement down the ligand/substrate gradient is expected when the diffusivity of the ligand/substrate-bound protein is higher than that of the unbound protein (negative chemotaxis). The work underscores the critical importance of measuring the diffusivity of the bound protein and compare it with that of the free protein.
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