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STRUCTURE OF MALTOSE TRANSPORTER: E COLI MEMBRANE ATP BINDING SUBUNIT

STRUCTURE OF MALTOSE TRANSPORTER: E COLI MEMBRANE ATP BINDING SUBUNIT
麦芽糖转运蛋白的结构:大肠杆菌膜 ATP 结合亚基
批准号:
6120587
负责人:
HOWARD A SHUMAN
金额:
$0.6万
依托单位国家:
美国
项目类别:
财政年份:
1999
资助国家:
美国
项目状态:
已结题
起止时间:
1999-04-01 至 2000-03-31

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中文摘要
翻译
他们相信他们已经用DNA构建了一个共价晶格 低聚物 建筑的基本单元是一个 反平行DNA双交换分子。 这些已经被结扎了 变成他们认为的I G床单 Ile第一次尝试 在STEM中发现的壁到壁蛋白酶K中, 用来停止结扎 第二次尝试发现, 缓冲区控制相当脏,因此无法区分 虽然它现在没有外来蛋白质。 在 在这两次尝试中,可以发现一些诱人的领域。进一步的工作 等待进一步纯化。 此外,他们还试图 在其中一个组分寡核苷酸的末端标记上11个金。 这应该是更好地可视化在干fl=他们的早期 尝试使用胶体金。
英文摘要
They believe they have built a 2-1) covalent lattice from DNA oligomers. The fundamental unit of the construction is an antiparallel DNA double crossover molecule. These have been ligated into what they believe are about I g sheets. Ile first attempt to visualize this in the STEM found wall-to-wall proteinase K which had been used to stop the ligation. The second attempt found that the buffer control was rather dirty and consequently indistinguishable from the sample, though it was now free of extraneous protein. In both tries, some tantalizing areas could be found. Further work awaits additional purification. In addition, they were trying to label the end of one of the component oligoiners with undecagold. This should be much better to visualize in the STEM fl= their early attempts using colloidal gold.
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