Biophysical characterization of fibroblast growth factor homologous factor-1b (FHF-1b): sodium dodecyl sulfate promotes two state folding.
Protein Pept Lett
; 15(2): 215-8, 2008.
Article
en En
| MEDLINE
| ID: mdl-18289114
The current article describes the biophysical characterization and folding studies of fibroblast growth factor homologous factor-1b (FHF-1b) in comparison with acidic fibroblast growth factor (FGF-1). Our data indicates that FHF-1 is significantly more stable than FGF-1. The folding mechanism of these two proteins seems to be different although they share high degree of sequence and structural similarity. FHF-1 unfolds through stable intermediate state while unfolding of FGF-1 is two-state. Interestingly, low concentration of sodium dodecyl sulfate (SDS) drives the folding pathway of FHF-1b to two-state.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Pliegue de Proteína
/
Factores de Crecimiento de Fibroblastos
Límite:
Humans
Idioma:
En
Revista:
Protein Pept Lett
Asunto de la revista:
BIOQUIMICA
Año:
2008
Tipo del documento:
Article
País de afiliación:
India
Pais de publicación:
Países Bajos