A novel method of analyzing proline synonymous codons in E. coli.
FEBS Lett
; 576(3): 336-8, 2004 Oct 22.
Article
em En
| MEDLINE
| ID: mdl-15498558
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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Códon
/
Prolina
/
Escherichia coli
Idioma:
En
Ano de publicação:
2004
Tipo de documento:
Article