Ligand-linked changes in the aggregation state of biological macromolecules occur and have importance in several physiological processes, e.g., the response of hormone receptors, cooperative ligand binding, and others. The mathematical formalisms that express the thermodynamics governing these processes are complex, as they are required to describe observations made under experimental conditions in which many parameters may be simultaneously varied. The description of the functional behaviour of proteins that present ligand-linked association-dissociation events must accommodate cases where both the binding stoichiometries and reaction mechanisms are variable. In this paper, we review some paradigmatic cases that cover different structural arrangements and binding modes, with special attention to the case of dissociating homodimeric transport proteins and receptors. Even though we cannot pretend to be comprehensive on the proteins presenting this behaviour, we believe that we can attempt to be comprehensive on the structural arrangements and thermodynamic properties of these systems, which fall into a limited set of possible types.

中文翻译：

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在转运蛋白和激素受体中的配体连接的缔合-解离。

发生与生物大分子聚集状态相关的配体变化，并且在几个生理过程中具有重要意义，例如，激素受体的响应，配体协同结合等。表示控制这些过程的热力学的数学形式是复杂的，因为它们需要描述在实验条件下可以同时改变许多参数的观察结果。呈现配体连接的缔合-解离事件的蛋白质功能行为的描述必须适应结合化学计量和反应机制均可变的情况。在本文中，我们回顾了一些涵盖不同结构安排和约束方式的范式案例，特别注意解离同型二聚体转运蛋白和受体的情况。即使我们不能假装对呈现这种行为的蛋白质不了解，但我们相信我们可以尝试对这些系统的结构安排和热力学性质进行全面了解，这些系统属于有限的一组可能的类型。