Nuclear magnetic resonance assignments and secondary structure of bovine S100 beta protein.
Nuclear magnetic resonance assignments and secondary structure of bovine S100 beta protein.
复制标题
牛 S100 β 蛋白的核磁共振分配和二级结构。
DOI：
10.1016/0014-5793(95)00296-l
复制
发表时间：
1995
期刊：
影响因子：
3.5
通讯作者：
Roberts,GC
中科院分区：
文献类型：
--
作者：
Kilby,PM;VanEldik,LJ;Roberts,GC
S100β is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium‐binding proteins containing the helix‐loop‐helix calcium binding motif. The structure of only one S100 protein, calbindin D9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium‐free S100β. The secondary structure is similar to that of calbindin D9k, determined using NMR, except that there is clear evidence for an additional well ordered 5‐residue α‐helix in S100β.
