@article { ISI:000352745300007,
	title = {Cloning, expression and in silico studies of a serine protease from a marine actinomycete (Nocardiopsis sp NCIM 5124)},
	journal = {Process Biochemistry},
	volume = {50},
	number = {3},
	year = {2015},
	month = {MAR},
	pages = {378-387},
	publisher = {ELSEVIER SCI LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<p>A serine protease (N. protease), from Nocardiopsis sp., was cloned and expressed in Escherichia coli and investigated for its potential kinetic stability. Protein expression using two vectors, pET-22b (+) and pET-39b (+) was compared based on proper folding and soluble expression of the protein. pET-39b (+) was found to be a better vector for soluble expression of this protease containing disulfide bonds. In silico studies were also carried out for N. protease. Homology modeling suggested N. protease to be a member of PA clan of proteases. The phylogenetic analysis showed relatedness of N. protease to kinetically stable proteases. Molecular docking studies performed exhibited interaction of a peptide substrate with catalytic pocket of the enzyme. High temperature MD simulations were performed on N. protease to study its unfolding behavior and comparisons were made with alpha LP. A novel approach to study {\textquoteleft}cooperativity{\textquoteright} of protein unfolding was undertaken, wherein {\textquoteleft}P{\textquoteright} value analysis based on phi and psi values of the protein was performed. Data showed sharper P value transition for alpha LP when compared to N. protease thus indicating relatively less kinetic stability of N. protease. Present study holds significance as the non-streptomycete actinomycetes group is least explored and ensures industrially important enzymes with exceptional stabilities. (C) 2015 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Actinomycetes, Cloning and expression, Kinetic stability, Protease, Thermal simulation},
	issn = {1359-5113},
	doi = {10.1016/j.procbio.2014.12.025},
	author = {Rohamare, Sonali and Gaikwad, Sushama M. and Jones, Dafydd and Bhavnani, Varsha and Pal, Jayanta and Sharma, Ranu and Chatterjee, Prathit}
}
