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|Title:||The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii|
|Citation:||Journal of Peptide Research, 1999; 54(2):137-145|
|Publisher:||MUNKSGAARD INT PUBL LTD|
|B.C.S. Chia, J.H. Bowie, J.A. Carver and T.D. Mulhern|
|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.|
|Keywords:||Antibiotic peptides; NMR spectroscopy; solution structure; toadlet; uperin 3.6; Uperoleia mjobergii|
|Rights:||© Munksgaard International Publishers Ltd, 1999|
|Appears in Collections:||Biochemistry publications|
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