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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels
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New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels

机译：通过捕获硅胶中不稳定的蛋白质构象，获得了变构机制的新见解

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摘要

To understand why the classical two-state allosteric model of Monod, Wyman, and Changeux explains cooperative oxygen binding by hemoglobin but does not explain changes in oxygen affinity by allosteric inhibitors, we have investigated the kinetic properties of unstable conformations transiently trapped by encapsulation in silica gels. Conformational trapping reveals that after nanosecond photodissociation of carbon monoxide a large fraction of the subunits of the T quaternary structure has kinetic properties almost identical to those of subunits of the R quaternary structure. Addition of allosteric inhibitors reduces both the fraction of R-like subunits and the oxygen affinity of the T quaternary structure. These kinetic and equilibrium results are readily explained by a recently proposed generalization of the Monod-Wyman-Changeux model in which a preequilibrium between two functionally different tertiary, rather than quaternary, conformations plays the central role.
机译：要了解为什么Monod，Wyman和Changeux的经典二态变构模型解释了血红蛋白的协同氧结合作用，却没有解释变构抑制剂的氧亲和力变化，我们研究了通过包埋在二氧化硅中而短暂捕获的不稳定构象的动力学性质。凝胶。构象俘获表明，在一氧化碳的纳秒光解离之后，T四级结构的大部分亚基具有几乎与R四级结构的亚基相同的动力学性质。添加变构抑制剂可降低R样亚基的比例和T季结构的氧亲和力。最近提出的Monod-Wyman-Changeux模型泛化模型很容易解释这些动力学和平衡结果，其中两个功能不同的叔构象而不是季构象之间的预平衡起着核心作用。

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