Characterization of PhaP Protein from Bacillus thuringiensis serovar indiana using software tools

Phasins (PhaP) are proteins normally associated with granules of polyhydroxyalkanoates (PHA), a biodegradable polymer accumulated by many bacteria as a reserve molecule. Physicochemical characteristics and experimental structure of Phasins are not yet available in the Protein Databank (PDB). Apart from their structural role as part of the PHA granule cover, different structural and regulatory functions have been found associated to many of them, and several biotechnological applications have been developed using phasin protein fusions. Despite their remarkable functional diversity, the structure of these proteins has not been analyzed except in very few studies. In this work, homology modeling approach was employed to derive structures for these proteins. A program meant for comparative modelling Phyre2 was utilized for the purpose. Expasy's Prot-param server and Cys_rec tool were used for physicochemical and functional characterization of these proteins.