Conclusion

In conclusion, we have found that HSP90 has a highly conserved sequence across the species that we have studied by using multiple sequence alignment and have supported this idea as we have found the same domains (HATPase_c and HTP90) in all species. Throughout our study of HSP90 and its functions in these species the reasons for its conservation are clear, its role as a molecular chaperone in aiding and supporting protein folding and therefore creating and maintaining protein function are extremely important and during stress conditions even more so by preventing damage to cells and the organism due to protein misfolding. We have also found other roles of HSP90 depending on the organism such as in mice embryo development, prevention of mutations and in the trafficking of ribosomal subunits in frogs.

In studying the structure of HSP90 we can identify and understand the the molecular mechanism of HSP90s activity and also compare the structure of HSP90 from different species such as Homosapiens and Plasmodium noting their remarkable similarities due to the conservation of the protein sequence.