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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Biophysical Characterization of Fibroblast Growth Factor Homologous Factor-1b (FHF-1b): Sodium Dodecyl Sulfate Promotes Two State Folding

Author(s): Vikash Kumar Dubey, Bishal Kumar Singh, Nandini Sarkar, Monu Pande, Medicherla Venkata Jagannadham, Vikash Kumar Dubey, Bishal Kumar Singh and Medicherla Venkata Jagannadham

Volume 15, Issue 2, 2008

Page: [215 - 218] Pages: 4

DOI: 10.2174/092986608783489535

Price: $65

Abstract

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.

Keywords: Physiochemical studies, stability, intermediate state, FHF


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