Heat shock proteins (HSPs) are the proteins which are present normally in the cell but theirexpression level increases under stress condition and are mainly divided into five groups, low molecularweight HSP (LMW HSP), HSP 60, HSP 70, HSP 90 and high molecular weight HSP (HMW HSP). All theseclasses of HSPs are highly conserved and ubiquitous in nature and hence serve as a good model forphylogenetic analysis. For the first time in this study,the sequence and structural analysis has been carriedout to predict evolution of HSPs. The results obtained clearly show higher degree of sequence and structuralconservation. HSP 60 and HSP 70 are highly conserved in terms of both sequence and structure alignmentin comparison to HSP 90. The minimum amino acid identity that has been observed between all thehomologous sequences is 32.46%, 38%, 23.60% for HSP 60, HSP 70 and HSP 90 respectively, indicatingHSP 70 as the most conserved protein family followed by HSP 60 and HSP 90 family. The structuralanalysis of these proteins showed dominance of beta sheets in HSP70 and helices in HSP 90. The detailedanalysis 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 andwarrants further detailed analysis at organism level.