Unusually stable helical kink in the antimicrobial peptide — A derivative of gaegurin

The structure of an active analog of the antibacterial peptide gaegurin was investigated by CD and NMR spectroscopy. The NOE connectivities showed that 21 out of 24 residues formed an α-helix despite the presence of a central proline. CD and NMR analysis indicates that the helix is in fast equilibri...

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Veröffentlicht in:	FEBS letters 1996-09, Vol.392 (3), p.309-312
Hauptverfasser:	Suh, Jeong-Yong, Lee, Keun-Hyeung, Chi, Seung-Wook, Hong, Seong-Yu, Choi, Byoung-Wook, Moon, Hong-Mo, Choi, Byong-Seok
Format:	Artikel
Sprache:	eng
Schlagworte:	9-fluorenylmethyloxycarbonyl Anti-Infective Agents - chemistry Circular Dichroism Fmoc Gaegurin Hydrogen Bonding Kink Magnetic Resonance Spectroscopy Models, Molecular NMR NOE NOESY nuclear Overhauser enhancement nuclear Overhauser enhancement spectroscopy one-dimensional Peptides - chemistry Peptides - pharmacology Protein Conformation reverse phase-high performance liquid chromatography RP-HPLC Structure-Activity Relationship TOCSY total correlation spectroscopy α-Helix
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