Sequence-specific assignments of proton NMR resonance peaks and analysis of secondary structural elements of LC1, a novel antibacterial polypeptide

Autor: Cheng-Hua, Shao, Jia-Peng, Zhu, Yuan, Cheng, Jin-Feng, Wang, Wei-Bin, Gong, Qing, Xu, Zhang-Liang, Chen, Guang-Ying, Lu
Rok vydání: 2002
Předmět:
Zdroj: Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica. 34(4)
ISSN: 0582-9879
Popis: 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.
Databáze: OpenAIRE