横纹金蛛包裹丝的葡萄状蛛丝蛋白（AcSp1）重复结构域的1H、13C和15N核磁共振谱峰归属
1H, 13C and 15N NMR assignments of the aciniform spidroin (AcSp1) repetitive domain of Argiope trifasciata wrapping silk.
作者信息
Xu Lingling, Tremblay Marie-Laurence, Meng Qing, Liu Xiang-Qin, Rainey Jan K
机构信息
Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai, People's Republic of China.
出版信息
Biomol NMR Assign. 2012 Oct;6(2):147-51. doi: 10.1007/s12104-011-9344-z. Epub 2011 Oct 12.
Spider silk is one of nature's most remarkable biomaterials due to extraordinary strength and toughness not found in today's synthetic materials. Of the seven types of silk, wrapping silk (AcSp1) is the most extensible of the types of silks and has no sequence similarity to the other types. Here we report the chemical shifts for the AcSp1 199 amino acid protein repeat unit and its anticipated secondary structure based on secondary chemical shifts.
蜘蛛丝是自然界中最非凡的生物材料之一，因其具有当今合成材料所没有的非凡强度和韧性。在七种蜘蛛丝类型中，包裹丝（AcSp1）是最具延展性的，且与其他类型的蜘蛛丝没有序列相似性。在此，我们报告了AcSp1 199个氨基酸蛋白质重复单元的化学位移及其基于二级化学位移预测的二级结构。
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