ORIGINAL RESEARCH ARTICLE | Aug. 19, 2020
Association of Blood Pressure with Fruit Chaat Likeness
Muhammad Imran Qadir, Muazam Jelani, Jawaria Iftikhar
Page no 138-139
Objective of the present study was to analyze association of blood pressure with fruit chaat likeness. A questionnaire was prepared about the fruit chaat likeliness. 200 participants were took part in this project. All these people were the students of postgraduate class. First of all we measured the blood pressure of all the participants and then took their views about the likeliness of fruit chaat. The present study showed that blood pressure and fruit chaat likeness have no scientific relationship.
ORIGINAL RESEARCH ARTICLE | Aug. 22, 2020
In Silico Analysis of Molecular Interaction of EhSir2a with its Interacting Proteins from Human Pathogen Entamoeba histolytica
Pinaki Biswas, Somasri Dam
Page no 140-155
The human pathogen, Entamoeba histolytica contains four Sir2 homologs in its genome. We have designed the 3D tertiary structure of EhSir2a and its interacting partners by comparative homology modeling and studied their interaction by molecular docking. Sir2 proteins are known to interact with their substrates through the deacetylase domain present in its C-terminus. Interestingly, EhSir2a contains a unique Zn finger domain at its N terminus and this is not present in any known Sir2 protein. This study shows that EhSir2a may interact with this N-terminal residue also. It interacts with its substrate, elongation factor EhEF2 through this zinc-finger domain. The interaction sites are different for alpha-tubulin homologs, the other substrates of EhSir2a identified by yeast two-hybrid library screening. The coordinate files of the best-modeled structure for EhSir2a and its interacting proteins were processed for protein-protein docking using ClusPro v2.0 and HawkDock server. Tyr432, Asn422, Arg408 residues of α-tubulin are essential for interaction with EhSir2a. Here we report that molecular interactions of EhSir2a with its interacting partners are not restricted to the conserved NAD+ dependent deacetylase domain; it may also involve the N-terminal residue.