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通过质子核磁共振研究人纤溶酶原中的结构域相互作用。

Domain interactions in human plasminogen studied by proton NMR.

作者信息

Teuten A J, Smith R A, Dobson C M

机构信息

Oxford Centre for Molecular Sciences, University of Oxford, UK.

出版信息

FEBS Lett. 1991 Jan 14;278(1):17-22. doi: 10.1016/0014-5793(91)80073-c.

DOI:10.1016/0014-5793(91)80073-c
PMID:1847112
Abstract

The NMR spectrum of miniplasminogen (V443-plasminogen) under conditions of acidic pH reveals a subset of particularly well-resolved resonances whose chemical shift values are closely similar to those of isolated kringle 5. The temperature dependence of the spectrum indicates that this set of resonances disappears in a single cooperative unfolding transition appropriate for kringle 5, whilst other broader resonances from the protease domain persist to higher temperature. These results provide evidence for significant structural and motional independence of the kringle and protease domains in spite of the short linker between these domains. The NMR spectrum of Glu1-plasminogen is closely similar to that of miniplasminogen under the same conditions. This suggests that the domain independence observed in miniplasminogen is maintained in the intact molecule.

摘要

在酸性pH条件下,微型纤溶酶原(V443 - 纤溶酶原)的核磁共振谱显示出一组分辨率特别高的共振峰,其化学位移值与分离的kringle 5的化学位移值非常相似。该谱图的温度依赖性表明,这组共振峰在适合kringle 5的单一协同解折叠转变中消失,而来自蛋白酶结构域的其他较宽的共振峰在更高温度下仍然存在。这些结果提供了证据,表明尽管kringle结构域和蛋白酶结构域之间的连接子很短,但它们在结构和运动上具有显著的独立性。在相同条件下,Glu1 - 纤溶酶原的核磁共振谱与微型纤溶酶原的核磁共振谱非常相似。这表明在微型纤溶酶原中观察到的结构域独立性在完整分子中得以维持。

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Domain interactions in human plasminogen studied by proton NMR.通过质子核磁共振研究人纤溶酶原中的结构域相互作用。
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