Linked Life Data

15498558

Source:http://linkedlifedata.com/resource/pubmed/id/15498558

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-10-22
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
576
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
336-8
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
A novel method of analyzing proline synonymous codons in E. coli.
pubmed:affiliation
The Key Laboratory of Industrial Biotechnology, Ministry of Education, Southern Yangtze University, Wuxi 214036, Jiangsu, China. wml_yh@yahoo.com.cn
pubmed:publicationType
Journal Article