Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/11338
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dc.contributor.authorChia, B.en
dc.contributor.authorCarver, J.en
dc.contributor.authorMulhern, T.en
dc.contributor.authorBowie, J.en
dc.date.issued1999en
dc.identifier.citationJournal of Peptide Research, 1999; 54(2):137-145en
dc.identifier.issn1397-002Xen
dc.identifier.issn1399-3011en
dc.identifier.urihttp://hdl.handle.net/2440/11338-
dc.description.abstractUperin 3.6 (GVIDA5AKKVV10NVLKN15LF-NH2) is a wide-spectrum antibiotic peptide isolated from the Australian toadlet, Uperoleia mjobergii. With only 17 amino acid residues, it is smaller than most other wide-spectrum antibiotic peptides isolated from amphibians. In 50% (by vol.) trifluoroethanol, an NMR study and structure calculations indicate that uperin 3.6 adopts a well-defined amphipathic α-helix with distinct hydrophilic and hydrophobic faces. Examination of the activities of synthetic modifications of uperin 3.6 reveal that the three lysine residues are essential for antibiotic activity.en
dc.description.statementofresponsibilityB.C.S. Chia, J.H. Bowie, J.A. Carver and T.D. Mulhernen
dc.language.isoenen
dc.publisherMUNKSGAARD INT PUBL LTDen
dc.rights© Munksgaard International Publishers Ltd, 1999en
dc.subjectAntibiotic peptides; NMR spectroscopy; solution structure; toadlet; uperin 3.6; Uperoleia mjobergiien
dc.titleThe solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergiien
dc.typeJournal articleen
dc.identifier.rmid0030004377en
dc.identifier.doi10.1034/j.1399-3011.1999.00095.xen
dc.identifier.pubid68383-
pubs.library.collectionBiochemistry publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
Appears in Collections:Biochemistry publications

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