In silico Characterization of Heat Shock Protein HSP27 in Mammals

Abstract

Dairy animals have a significant role in every country’s agricultural economy. Livestock is the major sub-sector of the agricultural industry and the value of dairy products is increasing globally. Under pathological circumstances heat shock proteins (HSPs) promote protein repair, folding, refolding of misfolded peptides, and possible breakdown of irreparable proteins. Heat shock protein 27 (HSP27) is a member of the small heat shock protein family (sHSPs) also called HSPB1. HSP27 is crucial in the regulation and progression of different types of tumors and also acts as an oncotherapeutic target in humans and other mammals especially sheep. By using computational tools, a detailed in silico investigation of HSP27 sequences from humans and sheep has been examined with respect to their structural, functional, expression and phylogenetic properties. An extensive study has been made to compare the human protein with that of other mammals using computational tools. However, the sequences of HSP27 in humans and sheep are closely linked with each other. Although the sequences of HSP27 vary, their structural characteristics and functional properties remain the same. In this study, hydrophilic proteins with an average molecular weight of 27kDa were discovered both in humans and sheep. This study helps to understand the economic worth of dairy animals worldwide. HSP27 phosphorylation has been predicted as an anticancer agent. Recent research shows that new strategies have been developed for cancer treatment based on therapy of HSP27. This research will highlight the characterization and significant role of HSP27 in sheep.