Biophysical Characterization of Fibroblast Growth Factor Homologous Factor-1b (FHF-1b): Sodium Dodecyl Sulfate Promotes Two State Folding
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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Document Type: Research Article
Publication date: 2008-02-01
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