Parnham Stuart, Gaines William A, Duggan Brendan M, Marcotte William R, Hennig Mirko
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, 173 Ashley Ave., BSB 535D, PO Box 250509, Charleston, SC 29425, USA.
Biomol NMR Assign. 2011 Oct;5(2):131-3. doi: 10.1007/s12104-010-9284-z. Epub 2010 Dec 10.
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 all (1)H, (13)C, and (15)N resonances in the 14 kDa N-terminal domain of major ampullate spidroin 1 (MaSp1-N) of the golden orb-web spider Nephila clavipes.
蜘蛛拖网丝的基本组成部分是由主要壶腹腺分泌的两种纤维蛋白，分别称为蜘蛛丝蛋白1和2（MaSp1、MaSp2）。这些蛋白质由一个大的中央结构域组成，该结构域由大约100个35 - 40个氨基酸的重复序列串联拷贝组成。非重复的N端和C端结构域位于重复核心的两侧，其中C端结构域被认为在纺丝过程中会从可溶状态转变为不可溶状态。由于克隆和表达困难，直到最近N端结构域在很大程度上仍不为人所知。在此，我们报告了金色圆蛛Nephila clavipes主要壶腹蜘蛛丝蛋白1（MaSp1 - N）14 kDa N端结构域中所有（1）H、（13）C和（15）N共振的近乎完全归属。
