Heat shock proteins (HSPs) such as HSP70A, HSP90 etc. (also known as Chaperons) play an important role in folding and unfolding of proteins, an assemblage of multiprotein complexes, transportation and sorting of proteins in subcellular compartments, cell cycle control, signaling pathways, protection against stress and programmed cell death. Studies have also linked heat shock proteins with a sudden rise in temperature, which can be related to anhydrobiosis in nematodes. Considering the significance of HSPs in nematodes and bacteria, the present study was designed for their in silico analysis in Caenorhabditis elegans and Photorhabdus temperata. The availability of a vast amount of sequence data generated through various bioinformatics tools, coupled with computational biology advancements, provides an ideal framework for silico gene expression and its analysis. A detailed in silico insight into these proteins include physicochemical properties, secondary structure prediction, homology modeling, and different models. The amino acid composition data were subjected to multivariate techniques, Pearson correlation, and phylogenetic analysis. In the present study, the authors characterized different HSPs according to different stability parameters and valid structures. A detailed in silico analysis of these proteins and prediction of their activity in different conditions can be very useful in both in vitro and in vivo experiments.
In silico analysis of the binding of anthelmintics to Caenorhabditis elegans P -glycoprotein 1