人类唾液蛋白N端片段的构型（英文）  

Conformation of the N-Terminal Fragment of Human Salivary Statherin

作　　者：郭玹铭 张七凤 陈振中[1] 

机构地区：[1]台湾大学化学系 [2]"中央研究院"基因体中心

出　　处：《波谱学杂志》2015年第2期283-290,共8页Chinese Journal of Magnetic Resonance

基　　金：The"National Science Council"(NSC 100-2628-M-002-009-MY3)

摘　　要：人类唾液蛋白Statherin是含有43残基的酸性磷酸化蛋白.此蛋白对磷酸钙具有较高的吸附性,已知其N端15残基的片段(SN-15)会吸附于磷灰石的表面.在该工作中,作者以液体核磁共振波谱学研究SN-15的分子结构.圆二色光谱显示SN-15在磷酸盐缓冲溶液中具α螺旋构型.根据高分辨核磁共振氢谱(COSY,TOCSY及NOESY)作者得到相关的NOE及J耦合数据,氢氘交换实验也进一步显示SN-15具α螺旋构型.Human salivary statherin is a 43-residue acidic phosphoprotein present in human saliva, possessing a high affinity for calcium phosphate minerals such as hydroxyapatite. The N-terminal 15-residue fragment of statherin （SN-15） is known to bind strongly to the crystallites of hydroxyapatite. In this work, we investigate the conformation of SN-15 in aqueous solution by NMR. Analysis of the CD spectra shows that SN-15 adopts ana-helical structure in phosphate buffer. High-resolution proton NMR spectra （COSY, TOCSY, and NOESY） have been acquired, from which the NOE patterns andJ-couplings of amide hydrogens have been obtained. Together with the constraints obtained from amide-hydrogen exchange experiments, the molecular structure of SN-15 has shown to be a continuousa-helical structure.

关 键 词：生物成矿 磷灰石 SN-15 

分 类 号：O482.53[理学—固体物理]