Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/11338
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DC Field | Value | Language |
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dc.contributor.author | Chia, B. | - |
dc.contributor.author | Carver, J. | - |
dc.contributor.author | Mulhern, T. | - |
dc.contributor.author | Bowie, J. | - |
dc.date.issued | 1999 | - |
dc.identifier.citation | Chemical Biology and Drug Design, 1999; 54(2):137-145 | - |
dc.identifier.issn | 1397-002X | - |
dc.identifier.issn | 1399-3011 | - |
dc.identifier.uri | http://hdl.handle.net/2440/11338 | - |
dc.description.abstract | Uperin 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. | - |
dc.description.statementofresponsibility | B.C.S. Chia, J.H. Bowie, J.A. Carver and T.D. Mulhern | - |
dc.language.iso | en | - |
dc.publisher | MUNKSGAARD INT PUBL LTD | - |
dc.rights | © Munksgaard International Publishers Ltd, 1999 | - |
dc.source.uri | http://dx.doi.org/10.1034/j.1399-3011.1999.00095.x | - |
dc.subject | Antibiotic peptides; NMR spectroscopy; solution structure; toadlet; uperin 3.6; Uperoleia mjobergii | - |
dc.title | The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1034/j.1399-3011.1999.00095.x | - |
pubs.publication-status | Published | - |
Appears in Collections: | Aurora harvest 2 Biochemistry publications |
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