Polyproline fold-In imparting kinetic stability to an alkaline serine endopeptidase.

@article{Rohamare2013PolyprolineFI,
  title={Polyproline fold-In imparting kinetic stability to an alkaline serine endopeptidase.},
  author={Sonali B. Rohamare and Vaishali Dixit and Pavan Kumar Nareddy and Dokku Sivaramakrishna and Musti J Swamy and Sushama M. Gaikwad},
  journal={Biochimica et biophysica acta},
  year={2013},
  volume={1834 3},
  pages={708-16}
}
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 transitions of the enzyme were studied under various denaturing conditions. Enzymatic activity of NprotI was stable in the vicinity of GdnHCl upto… CONTINUE READING