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A novel approach for the evaluation of positive cooperative guest binding: Kinetic consequences of structural tightening

机译:评估积极的合作伙伴绑定的一种新颖方法:结构收紧的动力学后果

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摘要

Cooperativity is one of the most relevant features displayed by biomolecules. Thus, one of the challenges in the field of supramolecular chemistry is to understand the mechanisms underlying cooperative binding effects. Traditionally, cooperativity has been related to multivalent receptors, but Williams etal. have proposed a different interpretation based on the strengthening of noncovalent interactions within receptors upon binding. According to such an interpretation, positive cooperative binding operates through structural tightening. Hence, a quite counterintuitive kinetic behavior for positively cooperative bound complexes may be postulated: the more stable the complex, the slower it is formed. Such a hypothesis was tested in a synthetic system in which positive cooperative binding was previously confirmed by calorimetric experiments. Indeed, a linear correlation between the thermodynamics (ΔG°) and the kinetics (ΔG~≠) of guest binding confirmed the expected behavior. These distinctive kinetics provide solid evidence of positive cooperative guest binding, which is particularly useful bearing in mind that kinetic experiments are frequently and accurately carried out in both synthetic and biological systems.
机译:合作性是生物分子显示的最相关的功能之一。因此,超分子化学领域的挑战之一是了解潜在的协同结合效应的机制。传统上,合作性与多价受体有关,但Williams等人。已经基于结合后受体内非共价相互作用的增强提出了不同的解释。根据这种解释,积极的合作约束通过结构性紧缩来进行。因此,可以假定对于正合作结合的复合物来说,其动力学行为是违反直觉的:复合物越稳定,其形成就越慢。这种假设在合成系统中进行了测试,在该系统中,先前已通过量热实验确认了积极的合作结合。实际上,客体结合的热力学(ΔG°)和动力学(ΔG-≠)之间的线性相关性证实了预期的行为。这些独特的动力学提供了积极的客体结合的确凿证据,尤其要记住动力学实验是在合成和生物系统中频繁且准确地进行的。

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