ABSTRACT-Heat shock proteins (HSPs) are the proteins which are present normally in the cell but their expression level increases under stress condition and are mainly divided into five groups, low molecular weight HSP (LMW HSP), HSP 60, HSP 70, HSP 90 and high molecular weight HSP (HMW HSP). All these classes of HSPs are highly conserved and ubiquitous in nature and hence serve as a good model for phylogenetic analysis. For the first time in this study,the sequence and structural analysis has been carried out to predict evolution of HSPs. The results obtained clearly show higher degree of sequence and structural conservation. HSP 60 and HSP 70 are highly conserved in terms of both sequence and structure alignment in comparison to HSP 90. The minimum amino acid identity that has been observed between all the homologous sequences is 32.46%, 38%, 23.60% for HSP 60, HSP 70 and HSP 90 respectively, indicating HSP 70 as the most conserved protein family followed by HSP 60 and HSP 90 family. The structural analysis of these proteins showed dominance of beta sheets in HSP70 and helices in HSP 90. The detailed analysis of all the HSP homologues revealed high conservation of glycine residues and ATP binding pockets. Thus this study has revealed that HSPs are highly structurally and functionally conserved proteins and warrants further detailed analysis at organism level.