Conformational changes induced by Mg2+ on the multiple forms of glutamine synthetase from Bacillus brevis Bb G1

dc.contributor.authorAbraham, Suja
dc.date.accessioned2024-05-26T15:40:38Z
dc.date.available2024-05-26T15:40:38Z
dc.date.issued2013-09-12
dc.description.abstractConformational 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+.
dc.identifier.issn1314-6246
dc.identifier.urihttps://doi.uni-plovdiv.bg/handle/"store"/60
dc.language.isoen
dc.publisherPlovdiv University Press “Paisii Hilendarski”
dc.subjectglutamine synthetase
dc.subjectfluorescence spectroscopy
dc.subjectconformational changes
dc.titleConformational changes induced by Mg2+ on the multiple forms of glutamine synthetase from Bacillus brevis Bb G1
dc.typeArticle
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