Structural evolution of human recombinant alpha B-crystallin under UV irradiation.
Biomacromolecules
; 9(2): 431-4, 2008 Feb.
Article
em En
| MEDLINE
| ID: mdl-18211002
ABSTRACT
External stresses cause certain proteins to lose their regular structure and aggregate. In order to clarify this abnormal aggregation process, a structural evolution of human recombinant alphaB-crystallin under UV irradiation was observed with in situ small-angle neutron scattering. The abnormal aggregation process was identified to fall in three time zones incubation, aggregation, and saturation. During the incubation time, the size of aggregates was almost unchanged but a deformation in the local structure was developing. After the incubation time, abnormal aggregation proceed. When the volume of the aggregates reached around twice the size as that of the initial aggregates, the aggregation rate slowed down, which marked the onset of saturation.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Raios Ultravioleta
/
Proteínas Recombinantes
/
Cadeia B de alfa-Cristalina
Limite:
Humans
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article