Nearly complete 1 H, 13 C and 15 N chemical shift assignment of monomeric form of N-terminal domain of Nephila clavipes major ampullate spidroin 2
Nearly complete 1 H, 13 C and 15 N chemical shift assignment of monomeric form of N-terminal domain of Nephila clavipes major ampullate spidroin 2
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棒络新妇大壶腹蛛丝蛋白 2 的 N 末端结构域单体形式几乎完成 1 H、13 C 和 15 N 化学位移分配
DOI：
10.1007/s12104-020-09972-5
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发表时间：
2020
影响因子：
0.9
通讯作者：
Keiji Numata
中科院分区：
文献类型：
--
作者：
Nur Alia Oktaviani;Ali D. Malay;Akimasa Matsugami;Fumiaki Hayashi;Keiji Numata
蜘蛛拖丝因其优异的机械性能而受到广泛认可。拖丝蛋白主要由两种蛋白质组成，即大壶状腺蛛丝蛋白1（major ampullate spidroin 1，MaSp 1）和大壶状腺蛛丝蛋白2（major ampullate spidroin 2，MaSp 2）。MaSp的N-末端结构域（NTD）构象显示出对离子和pH梯度的强烈依赖性，这对蜘蛛丝的自组装行为至关重要。在蜘蛛大壶腹腺中，其中pH值为中性，NaCl浓度高，NTD形成单体。相比之下，在纺丝导管内，其中pH变得更酸性（至pH ~ 5）并且盐浓度低，NTD以反平行取向形成二聚体。在这项研究中，我们报告了近完整的骨干和侧链化学位移分配的单体形式的NTD的MaSp 2 fromNephila clavipesat pH 7在300 mM NaCl的存在下。我们的NMR数据表明，单体形式的NTD MaSp 2的二级结构由五个螺旋区域组成。
Spider dragline silk is well recognized due to its excellent mechanical properties. Dragline silk protein mainly consists of two proteins, namely, major ampullate spidroin 1 (MaSp1) and major ampullate spidroin 2 (MaSp2). The MaSp N-terminal domain (NTD) conformation displays a strong dependence on ion and pH gradients, which is crucial for the self-assembly behavior of spider silk. In the spider major ampullate gland, where the pH is neutral and concentration of NaCl is high, the NTD forms a monomer. In contrast, within the spinning duct, where pH becomes more acidic (to pH ~ 5) and the concentration of salt is low, NTD forms a dimer in antiparallel orientation. In this study, we report near-complete backbone and side chain chemical shift assignment of the monomeric form of NTD of MaSp2 fromNephila clavipesat pH 7 in the presence of 300 mM NaCl. Our NMR data demonstrate that secondary structure of monomeric form of NTD MaSp2 consists of five helix regions.