Shao Cheng-Hua, Zhu Jia-Peng, Cheng Yuan, Wang Jin-Feng, Gong Wei-Bin, Xu Qing, Chen Zhang-Liang, Lu Guang-Ying
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, China.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2002 Jul;34(4):457-62.
LC1 is a type of novel antibacterial polypeptide secreted by a Bacillus subtilis strain. It consists of 47 residues. Using bioengineering, LC1 was expressed in E.coli DH5alpha by using recombinant plasmid PBVAB16. By means of two-dimensional DQF-COSY, TOCSY and NOESY spectroscopies, protons of all 47 residues are identified. The studies show that the secondary structures of LC1 are principally anti-parallel beta sheets and extended conformations. It was speculated that there may be a hydrophobic core around Trp(23) in its three-dimensional structure.
LC1是一种由枯草芽孢杆菌菌株分泌的新型抗菌多肽。它由47个氨基酸残基组成。利用生物工程技术，通过重组质粒PBVAB16在大肠杆菌DH5α中表达了LC1。借助二维DQF - COSY、TOCSY和NOESY光谱，鉴定出了所有47个残基的质子。研究表明，LC1的二级结构主要是反平行β折叠和伸展构象。据推测，其三维结构中色氨酸（23）周围可能存在一个疏水核心。
