Thirunavukkarasu Sivaraman

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Understanding the relationships between conformations of proteins and their stabilities is one key to address the protein folding paradigm. The free energy change (ΔG) of unfolding reactions of proteins is measured by traditional denaturation methods and native hydrogen-deuterium (H/D) exchange methods. However, the free energy of unfolding (ΔG(U)) and the(More)
The present study appraised hepatoprotective activity of Aegle marmelos (L.) corr. leaf powder (crude) against carbon tetrachloride-induced hepatic damage in albino rats. The effect of the leaf powder on functioning against carbon tetrachloride (CCl 4)-induced hepatic damage was studied by assessing the biochemical parameters such as alanine transaminase(More)
Leptospirosis is a worldwide waterborne zoonosis caused by Leptospira interrogans serovar lai strain 56601 and no specific antibiotics are available to effectively treat the disease to date. The enzyme 3-methyladenine-DNA glycosylase I (LiTagA), which excises 3-methyadenine and 3-methylguanine from alkylated DNA, is an indispensable component for the(More)
Estimation of extrinsic (k ex) and intrinsic (k rc) exchange rate constants for labile protons of proteins is indispensable to determine the residue-specific free energies. While k ex of labile protons in proteins are determined by experimental methods, the k rc of those protons are calculated based on the parameters derived from the model compound studies,(More)
The unfolding kinetics of cardiotoxin analogue VI from Taiwan cobra (Naja naja atra) have been studied at 473 K, pH 7.0 in the presence of 0.1 M NaCl using molecular dynamics simulations for 50 ns. Trajectory structures stored at every 25 ps (2000 structures) were probed at molecular (RMSD and radius of gyration) and residue (RMSF, surface area(More)
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