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TitleSolution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: The role of charges and hydrogen bonding interactions in stabilizing helix conformations
Journal, issue, pagesPeptides, Vol. 29, Page 1633-1644, Year 2008
Publish dateMay 24, 2007 (structure data deposition date)
AuthorsResende, J.M. / Moraes, C.M. / Prates, M.V. / Cesar, A. / Almeida, F.C. / Mundim, N.C. / Valente, A.P. / Bemquerer, M.P. / Pilo-Veloso, D. / Bechinger, B.
External linksPeptides / PubMed:18656510
MethodsNMR (solution)
Structure data

PDB-2jpy:
Phylloseptin-2
Method: SOLUTION NMR

PDB-2jq0:
Phylloseptin-1
Method: SOLUTION NMR

PDB-2jq1:
Phylloseptin-3
Method: SOLUTION NMR

KeywordsANTIMICROBIAL PROTEIN / alpha helix / amphipathic character / C-Terminal Carboxyamidation / alpha-helix

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