NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
复制标题
Nephila clavipes spidroin 1 N 末端结构域的 NMR 分配。
DOI：
10.1007/s12104-010-9284-z
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发表时间：
2011
影响因子：
0.9
通讯作者：
Hennig,Mirko
中科院分区：
文献类型：
--
作者：
Parnham,Stuart;Gaines,WilliamA;Duggan,BrendanM;MarcotteJr,WilliamR;Hennig,Mirko
蜘蛛拖丝的组成部分是由壶腹腺分泌的两种纤维蛋白，分别称为蜘蛛蛋白1和2 （MaSp1, MaSp2）。这些蛋白质由大约100个35-40个氨基酸重复序列的串联拷贝组成一个大的中心结构域。非重复的N和c端结构域，其中c端结构域涉及在旋转过程中从可溶性和不可溶性状态转变，位于重复核心的侧面。由于克隆和表达的困难，直到最近n端结构域在很大程度上是未知的。在这里，我们报告了金球网蜘蛛nephila clavipes的主壶腹蛛蛋白1 （MaSp1-N）的14 kDa n端结构域的所有1h，13C和15n共振的几乎完整分配。
The building blocks of spider dragline silk are two fibrous proteins secreted from the major ampullate gland named spidroins 1 and 2 (MaSp1, MaSp2). These proteins consist of a large central domain composed of approximately 100 tandem copies of a 35–40 amino acid repeat sequence. Non-repetitive N and C-terminal domains, of which the C-terminal domain has been implicated to transition from soluble and insoluble states during spinning, flank the repetitive core. The N-terminal domain until recently has been largely unknown due to difficulties in cloning and expression. Here, we report nearly complete assignment for all1H,13C, and15N resonances in the 14 kDa N-terminal domain of major ampullate spidroin 1 (MaSp1-N) of the golden orb-web spiderNephila clavipes.