1H NMR studies of calmodulin. Resonance assignments by use of tryptic fragments.
1H NMR studies of calmodulin. Resonance assignments by use of tryptic fragments.
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钙调蛋白的 1H NMR 研究。
DOI：
10.1111/j.1432-1033.1984.tb07913.x
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Witold Drabikowski
中科院分区：
文献类型：
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作者：
David C. Dalgarno;R. Klevit;Barry A. Levine;Robert J. P. Williams;Zbigniew Dobrowolski;Witold Drabikowski
两个胰蛋白酶片段的钙离子结合蛋白钙调素已研究了高分辨率1H NMR。TR 1C（残基1 - 77）跨越蛋白质的前两个结构域，TR 2C（残基78 - 148）跨越后两个结构域。光谱表明，每个双结构域肽假定的构象是非常接近的天然蛋白质。这种特性在存在和不存在Ca 2+离子的情况下都成立。因此，相对简单的片段光谱获得的共振分配可以用来分配整个钙调素的光谱。几个指定的共振的化学位移模式和核Overhauser增强效应的分析表明，每一半的钙调素可以建模后，两个EF-手钙离子结合蛋白的晶体结构，即小白蛋白和肠钙离子结合蛋白。
Two tryptic fragments of the Ca2+ -binding protein calmodulin have been studied by high-resolution 1H NMR. TR1C (residues 1 - 77) spans the first two domains of the protein and TR2C (residues 78 - 148) spans the second two domains. The spectra indicate that each of the two-domain peptides assumes a conformation which is very close to that in the native protein. This characteristic holds both in the presence and in the absence of Ca2+ ions. Therefore, the resonance assignments obtained for the relatively simpler fragment spectra can be used to assign the spectrum of whole calmodulin. Analysis of the chemical shift patterns and nuclear Overhauser enhancement effects of several assigned resonances indicates that each half of calmodulin can be modelled after the two EF-hand Ca2+-binding proteins for which crystal structures are available, namely parvalbumin and intestinal Ca2+-binding protein.