Sequence‐specific assignments of downfield‐shifted amide proton resonances of calmodulin Use of two‐dimensional NMR analysis of its tryptic fragments
Sequence‐specific assignments of downfield‐shifted amide proton resonances of calmodulin Use of two‐dimensional NMR analysis of its tryptic fragments
复制标题
钙调蛋白低场位移酰胺质子共振的序列特异性分配 使用其胰蛋白酶片段的二维 NMR 分析
DOI：
10.1016/0014-5793(87)81182-1
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发表时间：
1987
期刊：
影响因子：
3.5
通讯作者：
K. Hikichi
中科院分区：
文献类型：
--
作者：
M. Ikura;O. Minowa;M. Yazawa;K. Yagi;K. Hikichi
应用二维核磁共振方法对钙调素1-75位残基的氨基端片段的500 MHz ~ 1H-NMR谱中极低场位移的酰胺质子共振进行了归属。完整钙调素的1H-NMR光谱的低场共振被分配到特定的氨基酸残基通过与残基1-75和78-148的胰蛋白酶片段的光谱比较，在Ca 2 +-游离和Ca 2 +-结合状态。研究了甘氨酸残基连接八面体Ca 2+配位位点Z和− Y位置上两个氨基酸残基的氢键作用。位点IV中的Gly 134显示出与位点I、II和III中分别涉及的其他甘氨酸25、61和98不同的性质。
Two-dimensional NMR methods were applied to assign the extremely downfield-shifted amide-proton resonances in the 500-MHz1H-NMR spectra of the NH2-terminal fragment of residues 1–75 of calmodulin. The low-field resonances of the1H-NMR spectra of intact calmodulin were assigned to specific amino acid residues by comparison with spectra of the tryptic fragments of residues 1–75 and 78–148, in both the Ca2+-free and Ca2+-bound states. The hydrogen bonding of glycine residues connecting the two amino acid residues at theZand −Ypositions in the octahedral Ca2+coordination site was investigated. The Gly 134 in site IV showed a different property from the other glycines, 25, 61 and 98, involved in sites I, II and III, respectively.