Insilico characterization, phylogenetic analysis and homology based 3D structural modeling of HSPA4 heat shock protein family a (Hsp70) member 4 from homo sapiens (human)

Abstract

HSP70 are the specialized Heat Shock Proteins that show their novelty presence inside the deepest part of Cellular Component Networks of Chaperons and involve with various heat Shock repairing up mechanisms as main Catalytic Components. They actively participate in proper alignment and resistance of all types pressures by their proper dealing with substrates and proper exposure of their hydrophobic peptide portions inside of their substrate molecules. The exchange of information cum process of information occurs between the cell components through HSP70’s low level of affinity ATP bind sites and High Affinity level of ADP binding sites. Therefore, ATP hydrolysis process plays a key role in fundamental mechanisms, in vitro and as well as in in vivo repairing mechanisms for the functioning of Chaperone like functionalities of HSP 70 proteins. In the current study analysis, Homology Modeling methods permits us for modeling the 3D structure of the protein by taking backbone of experimentally determined 3D-Structures of homologous proteins extracted in various structural formats like PDBs. We worked with HSPA4 heat shock protein family A (HSP 70) part 4 from Homo sapiens (Human) and conducted 3-D structure prediction using an Automated Swiss Model Generation by employing the crystal structures of Template molecule. PDB Blast and Template search for required protein were conducted with help of all the parameters with respect to Imapact and Psi Impact angles and that leads to for most noteworthy sequence identity, structural alignments and functionalities. Finally, the homology modeling were performed by using SWISS modeler and modeled proteins were fine tuned by using the Ramachandran Plot, by using PROCHECK and 3D-Check Software Programs.