| Literature DB >> 12590458 |
Shuryo Nakai1, Judy C K Chan, Eunice C Y Li-Chan, Jinglie Dou, Masahiro Ogawa.
Abstract
A new method, homology similarity analysis (HSA), was developed to investigate homology pattern similarities of selected segments within sequences of peptides. This new approach facilitated elucidation of the structure-function relationships of lactoferricin derivatives. Helix propensity of positions 4-9 in the lactoferricin sequence was the most important in determining the antimicrobial activity of lactoferricin against Escherichia coli, followed by cationic charge pattern at positions 4-9 and 1-3. The pattern similarity of segments within sequences could be a useful tool for representing the distribution attributes of amino acid residue properties to the structure-function relationships of proteins and peptides, especially when used in conjunction with principal component similarity analysis followed by the regression version of artificial neural networks.Entities:
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Year: 2003 PMID: 12590458 DOI: 10.1021/jf0206062
Source DB: PubMed Journal: J Agric Food Chem ISSN: 0021-8561 Impact factor: 5.279