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Multiple Sequence Alignment
FASTA sequences from the various organisms were aligned together in order to identify conserved domain sequences between the different human isoforms A1 and B and between representative protein sequences from other organisms. Black highlighted proteins are conserved - they are the same protein in all the sequences. Grey highlighted proteins indicate that the protein is not the same but has similar properties to the protein that is conserved in the other sequences (e.g. the conserved protein in 5 of the sequences may be I-Isoleucine but the last sequence has V-Valine which is grey as it shares hydrophobic side chain properties). White/Non highlighted proteins do not share any similarities and proteins not present at all in the sequence are marked as a hyphen '-'.
Here we can see that the sequences share large similarities, evidencing a highly conserved protein sequence for Hsp90 even through evolution. The MSA conducted was used to compare the different species’ isoform of Hsp90 protein. From this we can infer on the homology between the isoforms and produce a phlyogenetic analysis (see phylogeny tree) on the sequences.
E.coli, as illustrated in the phylogeny tree, is the furthest away from the evolution origin which is shown in the MSA by the many discrepancies between the its protein sequence and the sequences for the other species. A possible reason for the lack of conservation in E. coli is that HtpG is not an essential protein in non heat shock conditions (Pubmed).
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