Conformational and ion-binding properties of cyclolinopeptide A isolated from linseed.
J Biosci
;
1987 Mar; 11(1-4): 473-484
Artículo
en Inglés
| IMSEAR
| ID: sea-160544
ABSTRACT
The conformation of the cyclic nonapeptide from linseed, cyclolinopeptide A in methanol and in acetonitrile has been elucidated by one- and two-dimensional nuclear magnetic resonance. The molecule is folded in a ß-turn conformation. Cyclolinopeptide A interacts and weakly complexes with Tb3+ (a Ca2+ mimic ion) with the metal ion positioned proximally to the Phe residue, but with no substantial structural alteration upon metal binding. Cyclolinopeptide A is also seen to aid the translocation of Pr3+ (another Ca2+ mimic) across unilamellar liposomes. However, cyclolinopeptide A does not phase transfer or act as an ionophore of calcium ion myself. Experiments using lanthanide ions thus do not necessarily indicate any ionophoretic ability of the complexone towards calcium ions.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Idioma:
Inglés
Revista:
J Biosci
Año:
1987
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS