Sonali B. Rohamare

Learn More
Polyproline II (PPII) fold, an unusual structural element was detected in the serine protease from Nocardiopsis sp. NCIM 5124 (NprotI) based on far UV circular dichroism spectrum, structural transitions of the enzyme in presence of GdnHCl and a distinct isodichroic point in chemical and thermal denaturation. The functional activity and conformational(More)
The kinetically stable alkaline serine protease from Nocardiopsis sp.; NprotI, possessing polyproline II fold (PPII) was characterized for its pH stability using proteolytic assay, fluorescence and Circular Dichroism (CD) spectroscopy, and Differential Scanning Calorimetry (DSC). NprotI was found to be functionally stable when incubated at pH 1.0, even(More)
The single tryptophan residue from Nocardiopsis sp. serine protease (NprotI) was studied for its microenvironment using steady state and time-resolved fluorescence. The emission maximum was observed at 353 nm with excitation at 295 nm indicating tryptophan to be solvent exposed. Upon denaturation with 6 M guanidinum thiocyanate (GuSCN) the emission maxima(More)
  • 1