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pubmed-article:18289114pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:18289114pubmed:articleTitleBiophysical characterization of fibroblast growth factor homologous factor-1b (FHF-1b): sodium dodecyl sulfate promotes two state folding.lld:pubmed
pubmed-article:18289114pubmed:affiliationDepartment of Biotechnology, Indian Institute of Technology, Guwahati-781039, Assam, India. vdubey@iitg.ernet.inlld:pubmed
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