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.
Dubey
Vikash Kumar
VK
Department of Biotechnology, Indian Institute of Technology, Guwahati-781039, Assam, India. vdubey@iitg.ernet.in
Singh
Bishal Kumar
BK
Sarkar
Nandini
N
Pande
Monu
M
Jagannadham
Medicherla Venkata
MV
D000595:Amino Acid Sequence; D016220:Fibroblast Growth Factor 1 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D005346:Fibroblast Growth Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D017510:Protein Folding; D016415:Sequence Alignment; D012967:Sodium Dodecyl Sulfate; D013501:Surface-Active Agents
C486356:FGF12 protein, human; D013501:Surface-Active Agents; D016220:Fibroblast Growth Factor 1; D012967:Sodium Dodecyl Sulfate; D005346:Fibroblast Growth Factors