title: A novel method of analyzing proline synonymous codons in E. coli.
abstract: Proline is a special imino acid in protein and the isomerization of the prolyl peptide bond has notable biological significance and influences the final structure of protein greatly, so the correlation between proline synonymous codon usage and local amino acid, the correlation between proline synonymous codon usage and the isomerization of the prolyl peptide bond were both investigated in the Escherichia coli genome by using a novel method based on information theory. The results show that in peptide chain, the residue at the first position C-terminal influences the usage of proline synonymous codon greatly and proline synonymous codons contain some factors influencing the isomerization of the prolyl peptide bond.
authors.affiliation: The Key Laboratory of Industrial Biotechnology, Ministry of Education, Southern Yangtze University, Wuxi 214036, Jiangsu, China. wml_yh@yahoo.com.cn
authors.forename: Ming-Lei
authors.initials: ML
authors.lastname: Wang
authors.forename: Jiang-Ning
authors.initials: JN
authors.lastname: Song
authors.forename: Wen-Bo
authors.initials: WB
authors.lastname: Xu
authors.forename: Wei-Jiang
authors.initials: WJ
authors.lastname: Li
mesh_terms: D003062:Codon / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D016680:Genome, Bacterial; D010455:Peptides / Q000737:chemistry; D011392:Proline / Q000235:genetics*; D011487:Protein Conformation
chemical_list: D003062:Codon; D010455:Peptides; D011392:Proline