Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor binding.
Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor binding.
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用于独立于模型确定蛋白质-DNA 相互作用平衡结合等温线的热力学方法：监测结合的光谱方法。
DOI：
10.1016/0076-6879(91)08017-c
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发表时间：
1991
影响因子：
--
通讯作者：
Bujalowski,W
中科院分区：
文献类型：
--
作者：
Lohman,TM;Bujalowski,W
通过监测配体或大分子的某些光谱性质的变化来测量配体与大分子相互作用的平衡结合常数是研究这些相互作用的常用方法。这是由于光谱方法的高灵敏度和应用这些实验程序的一般容易。此外，结合可以连续监测，从而便于动力学测量。这些方法的主要问题在于光谱信号是结合的间接度量，因为光谱信号的变化和结合程度之间的关系是未知的，是先验的。一种常见的方法是假设信号变化与配体或大分子的分数饱和度之间存在严格的比例关系；然而，通常情况下，这种直接的比例关系并不成立。在本章中，我们回顾了使用间接光谱技术来分析配体-大分子平衡滴定的方法。这些分析方法产生了热力学严格的、与模型无关的结合等温线，因此不需要假设信号变化与结合程度之间的关系。实际上，这些方法也可以用来定量地确定信号变化与平均结合程度之间的关系。此外，这里讨论的方法是一般的，不限于光谱信号，因此可以与任何强烈的物理化学性质，反映结合使用。
The measurement of equilibrium binding constants for ligand-macromolecule interactions by monitoring a change in some spectral property of the ligand or the macromolecule is a common method used to study these interactions. This is due to the high sensitivity of the spectroscopic methods and general ease in applying these experimental procedures. In addition, binding can be monitored continuously, thus facilitating kinetic measurements. The main problem with these methods results from the fact that the spectroscopic signal is an indirect measure of binding, since the relationship between the change in the spectroscopic signal and the extent of binding is unknown, a priori. A common recourse is to assume a strict proportionality between the signal change and the fractional saturation of the ligand or macromolecule; however, it is often the case that such a direct proportionality does not hold. In this chapter we have reviewed the use of methods to analyze ligand-macromolecule equilibrium titrations that are monitored by indirect spectroscopic techniques. These methods of analysis yield thermodynamically rigorous, model-independent binding isotherms, hence assumptions concerning the relationship between the signal change and the extent of binding are not required. In fact, these methods can also be used to determine quantitatively the relationship between the signal change and the average degree of binding. In addition, the approaches discussed here are general and not limited to spectroscopic signals and therefore can be used with any intensive physicochemical property that reflects binding.
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直接测量大肠杆菌 lac 阻遏物与非操作者 DNA 结合的关联常数。
影响因子：
2.9
作者：
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通讯作者：
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作者：
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关于大配体与一维均质晶格的协同结合：广义三态晶格模型
影响因子：
2.9
作者：
W. Bujalowski;T. Lohman;Charles Anderson
通讯作者：
Charles Anderson
DOI：
10.1016/s0021-9258(18)68829-5
发表时间：
1988-04
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
W. Bujalowski;Leslie B. Overman;T. Lohman
通讯作者：
W. Bujalowski;Leslie B. Overman;T. Lohman
影响因子：
2.9
作者：
CROTHERS, DM
通讯作者：
CROTHERS, DM