15N NMR assignments and chemical shift analysis of uniformly labeled 15N calbindin D9k in the apo, (Cd2+)1 and (Ca2+)2 states.
15N NMR assignments and chemical shift analysis of uniformly labeled 15N calbindin D9k in the apo, (Cd2+)1 and (Ca2+)2 states.
复制标题
均匀标记的 15N 钙结合蛋白 D9k 在 apo、(Cd2 )1 和 (Ca2 )2 状态下的 15N NMR 归属和化学位移分析。
DOI：
10.1016/0014-5793(92)80505-b
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发表时间：
1992
期刊：
影响因子：
3.5
通讯作者：
Chazin,WJ
中科院分区：
文献类型：
--
作者：
Skelton,NJ;Akke,M;Kördel,J;Thulin,E;Forsén,S;Chazin,WJ
15 N已被均匀地掺入EF-手Ca ~（2+）-结合蛋白calbindin D9 k中，因此异源实验可用于进一步表征该蛋白的apo、（Cd ~（2+））1和（Ca ~（2+））2状态的结构和动力学。的15 N NMR共振分配的2D 15 N-resolved 1H实验，这也允许识别的一些顺序和中程1H单键1H接触，被掩盖的化学位移简并在homopolymerization实验。15 N化学位移与蛋白质二级结构的相关性进行了分析。此外，apo→（Cd ~（2+））_1 →（Ca ~（2+））_2结合序列的~（15）N化学位移的变化证实了对蛋白质的作用主要与第一离子的螯合作用有关。
15N has been uniformly incorporated into the EF-hand Ca2+-binding protein calbindin D9kso that heteronuclear experiments can be used to further characterize the structure and dynamics of the apo, (Cd2+)1and (Ca2+)2states of the protein. The15N NMR resonances were assigned by 2D15N-resolved1H experiments, which also allowed the identification of a number of sequential and medium-range1Hsingle bond1H contacts that are obscured by chemical shift degeneracy in homonuclear experiments. The15N chemical shifts are analyzed with respect to correlations with protein secondary structure. In addition, the changes in15N chemical shift found for the apo→(Cd22+)1→(Ca2+)2binding sequence confirm that the effects on the protein are mainly associated with chelation of the first ion.