Sequence-specific assignments of proton NMR resonance peaks and analysis of secondary structural elements of LC1, a novel antibacterial polypeptide.
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.
Shao
Cheng-Hua
CH
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, China. lugy@pku.edu.cn
Zhu
Jia-Peng
JP
Cheng
Yuan
Y
Wang
Jin-Feng
JF
Gong
Wei-Bin
WB
Xu
Qing
Q
Chen
Zhang-Liang
ZL
Lu
Guang-Ying
GY
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D001412:Bacillus subtilis / Q000737:chemistry; D001419:Bacteria / Q000187:drug effects; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D017433:Protein Structure, Secondary; D020539:Sequence Analysis, Protein / Q000379:methods
D000900:Anti-Bacterial Agents; D010455:Peptides