{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T03:14:11Z","timestamp":1761707651125},"reference-count":0,"publisher":"Oxford University Press (OUP)","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2004,4,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Sequences of 221 \u03b1-helical antimicrobial peptides (\u03b1AMPs) were compared and 63\u2013166 of them were selected and analyzed using Perl programs. The results showed that aliphatic amino acids Gly, Leu, Ala, Ile and two positively charged amino acids Lys and Arg were composed of more than 63% of the first 20 residues of \u03b1AMPs. The weighed mean membrane partitioning energies at positions from 1 to 25 of \u03b1AMPs were calculated. Profile of the partitioning energies suggests oblique membrane insertion and an amphipathic \u03b1-helical structure of the N-terminus of \u03b1AMP (residues from 1 to 13), a bend structure at positions 13 and 14, and a less structured C-terminus that parallels the surface of the membrane. These structural features are in good agreement with the experimentally determined membrane structure of hemagglutinin fusion peptide from influenza virus. We hypothesize that this (N-terminal oblique \u03b1-helix)\u2014central bend\u2014(C-terminus) could be a common structural motif of membrane-disruptive peptides.<\/jats:p>","DOI":"10.1093\/bioinformatics\/bth027","type":"journal-article","created":{"date-parts":[[2004,3,2]],"date-time":"2004-03-02T21:41:06Z","timestamp":1078263666000},"page":"970-973","source":"Crossref","is-referenced-by-count":7,"title":["Sequence analysis and membrane partitioning energies of \u03b1-helical antimicrobial peptides"],"prefix":"10.1093","volume":"20","author":[{"given":"Xing","family":"Han","sequence":"first","affiliation":[{"name":"DuPont Haskell Laboratory for Health and Environmental Sciences, P.O. Box 50, Newark, DE 19714, USA"}]},{"given":"Wenjun","family":"Kang","sequence":"additional","affiliation":[{"name":"DuPont Haskell Laboratory for Health and Environmental Sciences, P.O. Box 50, Newark, DE 19714, USA"}]}],"member":"286","published-online":{"date-parts":[[2004,2,5]]},"container-title":["Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/20\/6\/970\/48905135\/bioinformatics_20_6_970.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/20\/6\/970\/48905135\/bioinformatics_20_6_970.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,25]],"date-time":"2023-01-25T17:58:24Z","timestamp":1674669504000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article\/20\/6\/970\/233545"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,2,5]]},"references-count":0,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2004,4,12]]}},"URL":"https:\/\/doi.org\/10.1093\/bioinformatics\/bth027","relation":{},"ISSN":["1367-4811","1367-4803"],"issn-type":[{"value":"1367-4811","type":"electronic"},{"value":"1367-4803","type":"print"}],"subject":[],"published-other":{"date-parts":[[2004,4,12]]},"published":{"date-parts":[[2004,2,5]]}}}