Abstract
Clustering accentuated matches and highly conserved domains between bacterial and human heat shock gene and protein.
Highlights
Heat shock proteins (Hsps) constitute a family of proteins expressed in virtually all living organisms by activating specific genes as a cellular response to exposure to several stressful conditions, including heat shock, cold, UV light, wound healing or tissue remodeling (Li and Srivastava, 2004)
Conformational patterns of the secondary structure of the bacterial HscA protein demonstrated the presence of 274 alpha helixes (44.41%), 89 extended strands (14.42%) and 253 random coils (41%) (Figure 2A), whereas 247 alpha helixes (47%), 113 extended strands (17.6%) and 281 random coils (43.77%) were preferentially predicted from human Hsp70 protein (Figure 2B)
The findings described in current study demonstrated accentuated amounts of matches between hscA and hsp70 genes, as well as highly conserved sites between bacterial HscA and human Hsp70 proteins during structural alignments of phylogenetically distant and evolutionarily quite divergent species (Figure 1)
Summary
Heat shock proteins (Hsps) constitute a family of proteins expressed in virtually all living organisms by activating specific genes as a cellular response to exposure to several stressful conditions, including heat shock, cold, UV light, wound healing or tissue remodeling (Li and Srivastava, 2004). The current study aimed to assess comparatively the conservation degree of residues of nucleotides of the hscA and hsp70 genes and amino acids of the HscA and Hsp70 proteins of E. coli and Homo sapiens, as well as investigate variations in the conformational pattern of their secondary structures among such proteins using Bioinformatics’ tools.
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