Abraham, Suja2024-05-262024-05-262013-09-121314-6246https://doi.uni-plovdiv.bg/handle/"store"/60Conformational changes play an important role in the function of proteins. Glutamine synthetase, an important enzyme of nitrogen metabolism, was purified under sporulating (GSala) and non-sporulating (GSpyr) conditions and the effect of Mg2+ on these multiple forms was studied by fluorescence spectroscopy to detect possible conformational changes that occur in the presenceof Mg2+. The substantial changes in the fluorescence emission maximum, fluorescence intensity and lifetime that occur in the presence of different concentrations of Mg2+, indicated major changes in molecular conformations in both forms of this enzyme. The fluorescent changes produced by the effect of Mg2+ in GSala was much more prominent than in GSpyr. These observations strongly support the possibility that GSala and GSpyr undergoes a conformational change on binding with Mg2+.englutamine synthetasefluorescence spectroscopyconformational changesConformational changes induced by Mg2+ on the multiple forms of glutamine synthetase from Bacillus brevis Bb G1Article