Sequence-specific Assignments of Proton NMR Resonance Peaks and Analysis of Secondary Structural Elements of LC1, a Novel Antibacterial Polypeptide

SHAO Cheng-Hua, ZHU Jia-Peng, CHENG Yuan¹, WANG Jin-Feng¹, 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; ¹National Laboratory of Biomacromoleucules, Institute of Biophysics, the Chinese Academy of Sciences, Beijing 100101, China )

Abstract    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 DH5α 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 β sheets and extended conformations. It was speculated that there may be a hydrophobic core around Trp²³ in its three-dimensional structure.
Key words    antibacterial polypeptide LC1; 2D-NMR; sequence-specific assignment; secondary structural elements

^*Corresponding author: Tel, 86-10-62765669; Fax, 86-10-62751526;
 e-mail, [email protected]