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PubMed · 15498558

A novel method of analyzing proline synonymous codons in E. coli.

Ming-Lei Wang·Jiang-Ning Song·Wen-Bo Xu·Wei-Jiang Li
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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.

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CodonEscherichia coliGenome, BacterialPeptidesProlineProtein ConformationJournal Article

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Ming-Lei Wang, Jiang-Ning Song, Wen-Bo Xu, Wei-Jiang Li. 2004-10-22. A novel method of analyzing proline synonymous codons in E. coli.. https://doi.org/10.1016/j.febslet.2004.09.034

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