The conformational status of a protein influences the aerobic photolysis of its tryptophan residues: melittin, beta-lactoglobulin and the crystallins.
Photochem Photobiol
; 51(3): 357-62, 1990 Mar.
Article
em En
| MEDLINE
| ID: mdl-2356231
ABSTRACT
We have studied the aerobic photolysis of the tryptophan residues of the proteins melittin and beta-lactoglobulin when the proteins are in ordered conformations and when they are in randomly coiled states. The results suggest that the conformational status of the protein is a factor that influences the photolysis of the constituent tryptophan residues. This point appears to be of relevance to the photo-oxidation of the tryptophan residues of the eye lens proteins crystallins.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Triptofano
/
Raios Ultravioleta
/
Venenos de Abelha
/
Cristalinas
/
Lactoglobulinas
/
Meliteno
Idioma:
En
Revista:
Photochem Photobiol
Ano de publicação:
1990
Tipo de documento:
Article
País de afiliação:
Índia