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

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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 alpha-helix despite the presence of a central proline. CD and NMR analysis indicates that the helix is in fast equilibrium with random coil, From chemical shift analysis of the amide protons, the distances of hydrogen bonding in the helix were calculated, and manifested obvious periodicity which implied a kink in the middle of the helix. 1D amide proton exchange experiments provided further evidence of an exceptionally stable kink. It is inferred that this kink is important not only to the function of the peptide but also to the early stage of the folding as a nucleation site.
Publisher
ELSEVIER SCIENCE BV
Issue Date
1996-09
Language
English
Article Type
Article
Keywords

PROTEIN SECONDARY STRUCTURE; PROLINE RESIDUES; CHEMICAL-SHIFTS; SKIN

Citation

FEBS LETTERS, v.392, no.3, pp.309 - 312

ISSN
0014-5793
URI
http://hdl.handle.net/10203/75464
Appears in Collection
CH-Journal Papers(저널논문)
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