首页> 外文期刊>Journal of the American Chemical Society >Pulsed ELDOR Determination of the Intramolecular Distance between the Metal Binding Sites in Dicupric Human Serum Transferrin and Lactoferrin
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Pulsed ELDOR Determination of the Intramolecular Distance between the Metal Binding Sites in Dicupric Human Serum Transferrin and Lactoferrin

机译:脉冲ELDOR测定双杯人血清转铁蛋白和乳铁蛋白中金属结合位点之间的分子内距离

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摘要

Serum transferrin (Tf) and lactoferrin (Lf) are members of an important group of iron-binding and transport proteins. A single polypeptide folds into two lobes of similar structure, each binding a single Fe~(3+) ion. The iron can be removed and replaced by a number of other metal ions, while retaining the overall protein structure. Of great interest is how these proteins interact with their bacterial and mammalian receptors and how changes to the tertiary structure upon binding ultimately lead to iron release.
机译:血清转铁蛋白(Tf)和乳铁蛋白(Lf)是重要的铁结合和转运蛋白组的成员。单个多肽折叠成两个相似结构的小叶,每个小叶结合一个Fe〜(3+)离子。可以除去铁,并用许多其他金属离子代替铁,同时保留整体蛋白质结构。这些蛋白质如何与其细菌和哺乳动物受体相互作用,以及结合后三级结构的变化最终导致铁释放,是引起人们极大关注的问题。

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