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Human glutathione synthetase residues Valine 44 and Valine 45 are required for subunit stability and negative cooperativity
Valine 44 and Valine 45 serve as important residues for human glutathione synthetase (hGS) function and stability given their location at the dimer interface of this enzyme. Computational studies suggest Val45 has more ...
Reaction of (Z)- and (E)-β-chlorocinnamohydroximoyl chlorides with methoxide ion
New α,β-unsaturated hydroximoyl chlorides and hydroximates were synthesized and characterized. 13C NMR, 1H NMR, IR and elemental analysis were determined for each new compound. The kinetics of methoxide ion substitution ...
The dimer loop and electrostatic interactions at the dimer interface of human glutathione synthetase
Human glutathione synthetase (hGS) is homodimeric and negatively cooperative toward its γ-glutamyl substrate making it a good model to study protein-protein interactions. The allosteric pathway between hGS active sites is ...
Understanding the conformations and stabilities of g-quadruplexes formed by human telomere sequence in ideal and less ideal solutions
The G-rich termini of human chromosomes, called telomeres, have the ability to form unique DNA structures called G-Quadruplexes, which have been implicated in certain cancer types and, as a result, have drawn researchers' ...
Investigations into the unfolding of a DNA quadruplex: Effect of loop sequence
Understanding of the human telomere and telomerase is expected to provide major insights into genome stability, cancer, and telomere-related diseases. Quadruplexes have been received as a potential target for anti-cancer ...