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Online Journal of Bioinformatics©
Volume 20(3): 245-271, 2019.
Sequence, structural and phylogenetic analysis of heat shock proteins (HSP) 60, 70 and 90.
Desai NS (MSc, PhD), Anshika Agarwal (MTech) and Sehul Uplap (MTech).
Padmashree Dr. DY Patil University, Department of Biotechnology and
Desai NS., Agarwal A, Uplap S., Sequence, structural and phylogenetic analysis of heat shock proteins (HSP) 60, 70 and 90, Onl J Bioinform., 20(3): 245-271, 2019. Heat shock proteins (HSPs) are cell proteins whose expression increases under stress. The proteins are classed as low molecular HSP60, 70, 90 or high molecular weight, are highly conserved and ubiquitous, and are thus a suitable model for phylogenetic analysis. Sequence and structural analysis of HSP’s were performed to predict evolution. HSP60 and 70 were highly conserved in terms of both sequence and structure alignment in comparison to HSP90. The minimum amino acid identity observed between the homologous sequences was 32.46% for HSP 60, 38%, for HSP 70 and 23.60% for HSP90 with HSP70 as the most conserved protein family. Structural analysis showed dominance of beta sheets in HSP70 and helices in HSP90. All the HSP homologues revealed high conservation of glycine residues and ATP binding pockets. We find that HSP’s are highly conserved proteins requiring further detailed analysis in organisms.
Key words: HSP 60, HSP70, HSP 90, sequence, structure, alignment, conserved and evolution.