Unusually stable helical kink in the antimicrobial peptide--a derivative of gaegurin.
FEBS Lett
; 392(3): 309-12, 1996 Sep 02.
Article
em En
| MEDLINE
| ID: mdl-8774869
ABSTRACT
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 a-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.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Coréia do Sul