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TitleNMR structures in different membrane environments of three ocellatin peptides isolated from Leptodactylus labyrinthicus.
Journal, issue, pagesPeptides, Vol. 103, Page 72-83, Year 2018
Publish dateDec 17, 2016 (structure data deposition date)
AuthorsGomes, K.A.G.G. / Dos Santos, D.M. / Santos, V.M. / Pilo-Veloso, D. / Mundim, H.M. / Rodrigues, L.V. / Liao, L.M. / Verly, R.M. / de Lima, M.E. / Resende, J.M.
External linksPeptides / PubMed:29596881
MethodsNMR (solution)
Structure data

PDB-5u9q:
Ocellatin-LB1
Method: SOLUTION NMR

PDB-5u9r:
Ocellatin-LB2, solution structure in TFE by NMR spectroscopy
Method: SOLUTION NMR

PDB-5u9y:
Ocellatin-F1
Method: SOLUTION NMR

PDB-5ua6:
Ocellatin-LB1, solution structure in SDS micelle by NMR spectroscopy
Method: SOLUTION NMR

PDB-5ua7:
Ocellatin-LB2, solution structure in SDS micelle by NMR spectroscopy
Method: SOLUTION NMR

PDB-5ua8:
Ocellatin-F1, solution structure in SDS micelle by NMR spectroscopy
Method: SOLUTION NMR

Source
  • leptodactylus labyrinthicus (frog)
  • leptodactylus knudseni (Knudsen's thin-toed frog)
KeywordsANTIMICROBIAL PROTEIN / OCELLATIN / ANTIMICROBIAL PEPTIDES / HELIX / AMPHIPATHIC CHARACTER / C-TERMINAL CARBOXYAMIDATION / ANTIMICROBIAL PEPTIDE / ALPHA HELIX

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