单分子动力学的一般方案2：泊松指示剂的信息含量
Generic Schemes for Single Molecule Kinetics 2: Information Content of the Poisson Indicator
摘要：
最近，我们描述了一种途径分析技术（论文1），用于分析基于首次通过时间分布的单分子动力学通用方案。在这里，我们采用这种方法来推导表达式的泊松指标，随机变化的措施（基本上相当于法诺因子和曼德尔的Q参数），为各种更新（无记忆）酶促反应。我们研究其对底物浓度的依赖性，而不假设所有步骤都遵循泊松动力学。拟合的前两个等待时刻的函数形式的基础上，我们表明，二阶，非泊松动力学一般是欠定的，但可以指定在某些情况下。对于一个任意的中间拓扑结构的酶促反应，我们确定了一个通用的最小值的泊松指标作为底物浓度的函数，它可以用来调整底物浓度的随机波动和估计的最大数量的基本连续链接在营业额周期。我们确定了一个局部最大值的泊松指标（相对于底物浓度）的更新过程中的竞争性结合的签名，无论是基板和抑制剂之间或多个基板之间。我们的分析探讨了泊松指标测量和微观动力学机制之间的丰富联系。
英文摘要：
Recently, we described a pathway analysis technique (paper 1) for analyzing generic schemes for single-molecule kinetics based upon the first-passage time distribution. Here, we employ this method to derive expressions for the Poisson indicator, a measure of stochastic variation (essentially equivalent to the Fano factor and Mandel's Q parameter), for various renewal (memoryless) enzymatic reactions. We examine its dependence on substrate concentration, without assuming all steps follow Poissonian kinetics. Based upon fitting to the functional forms of the first two waiting time moments, we show that, to second order, the non-Poissonian kinetics are generally underdetermined but can be specified in certain scenarios. For an enzymatic reaction with an arbitrary intermediate topology, we identify a generic minimum of the Poisson indicator as a function of substrate concentration, which can be used to tune substrate concentration to the stochastic fluctuations and estimate the largest number of underlying consecutive links in a turnover cycle. We identify a local maximum of the Poisson indicator (with respect to substrate concentration) for a renewal process as a signature of competitive binding, either between a substrate and an inhibitor or between multiple substrates. Our analysis explores the rich connections between Poisson indicator measurements and microscopic kinetic mechanisms.
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