| http://purl.uniprot.org/citations/10424354 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10424354 | http://www.w3.org/2000/01/rdf-schema#comment | "In order to elucidate the structure-antibiotic activity relationships of the peptides, the three-dimensional structures of two hybrid peptides, CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) in trifluoroethanol-containing aqueous solution were investigated by NMR spectroscopy. Both CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) have strong antibacterial activity but only CA(1-8) - ME(1-12) has hemolytic activity against human erythrocytes. CA(1-8) - MA(1-12) has a hydrophobic 310-helix of only two turns combined with one short helix in the N-terminus with a flexible hinge section in between. CA(1-8) - MA(1-12) has a severely bent structure in the middle of the peptide. These structural features as well as the low hydrophobicity of CA(1-8) - MA(1-12) seem to be crucial for the selective lysis against the membrane of prokaryotic cells. CA(1-8) - ME(1-12) has an alpha-helical structure of about three turns in the melittin domain and a flexible structure with one turn in the cecropin domain connected with a flexible hinge section in between, and these might be the structural features required for membrane disruption against prokaryotic and eukaryotic cells. The central hinge region (Gly9-Ile10-Gly11) in an amphipathic antibacterial peptide is considered to play an important role in providing the conformational flexibility required for ion channel formation of the C-terminal hydrophobic alpha-helix on cell membrane."xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.org/dc/terms/identifier | "doi:10.1034/j.1399-3011.1999.00067.x"xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/author | "Kim Y."xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/author | "Shin S.Y."xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/author | "Hahm K.S."xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/author | "Oh D."xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/author | "Kang J.H."xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/author | "Kim K.L."xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/name | "J Pept Res"xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/pages | "578-589"xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/title | "NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A (1-8) - melittin (1-12) hybrid peptides."xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://purl.uniprot.org/core/volume | "53"xsd:string |
| http://purl.uniprot.org/citations/10424354 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10424354 |
| http://purl.uniprot.org/citations/10424354 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10424354 |
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| http://purl.uniprot.org/uniprot/#_P11006-mappedCitation-10424354 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10424354 |
| http://purl.uniprot.org/uniprot/P11006 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10424354 |
| http://purl.uniprot.org/uniprot/P01507 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10424354 |