ON NATURE OF ALLOSTERIC TRANSITIONS - IMPLICATIONS OF NON-EXCLUSIVE LIGAND BINDING
ON NATURE OF ALLOSTERIC TRANSITIONS - IMPLICATIONS OF NON-EXCLUSIVE LIGAND BINDING
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DOI：
10.1016/0022-2836(66)90097-0
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发表时间：
1966-01-01
影响因子：
5.6
通讯作者：
CHANGEUX, JP
中科院分区：
文献类型：
--
作者：
RUBIN, MM;CHANGEUX, JP
进一步的预测源自 Monod、Wyman 和 Changeux (1965) 的变构转变模型，该模型适用于一般情况，其中变构蛋白的两种假定构象状态以显着但不相等的亲和力（非排他性结合）结合特定配体。特别是，一种或多种配体（例如调节酶的底物、抑制剂或激活剂）的非排他性结合预计会引入限制：在它们存在的情况下，蛋白质构象状态之间的平衡可能改变的程度；每个配体饱和度的协同程度（通过希尔系数测量）；以及各种配体之间合作或拮抗相互作用的程度（部分和多价效应）。
Further predictions are derived from the model for allosterlc transitions of Monod, Wyman and Changeux (1965) for the general case in which both the postulated conformational states of an allosteric protein bind a specified ligand with significant but unequal affinity (non-exclusive binding). In particular, the non-exclusive binding of one or more of the ligands, such as the substrate, inhibitor or activator of a regulatory enzyme, is expected to introduce limits on: the extent to which the equilibrium between the conformational states of the protein may be shifted in their presence; the degree of co-operativity in the saturation by each ligand (as measured by the Hill coefficient); and the extent of co-operative or antagonistic interactions among the various ligands (partial and multivalent effects).