Fluorescence study on ligand induced conformational changes of glutamine synthetase from Bacillus brevis Bb G1 under sporulating conditions

dc.contributor.authorAbraham, Suja
dc.date.accessioned2024-05-28T17:47:03Z
dc.date.available2024-05-28T17:47:03Z
dc.date.issued2015-02-18
dc.description.abstractGlutamine synthetase, an important enzyme of nitrogen metabolism, was purified under sporulating conditions (GSala). The effect of ligands on the tryptophan fluorescence of the purified enzyme GSala was investigated. With increasing concentrations of L-glutamine in GSala, a blue shift in emission maximum with an increase in fluorescence intensity and decrease in life times were observed compared to the emission maximum, fluorescence intensity and life times of GSala. With increasing concentrations of glycine in GSala, a shift in emission maximum, change in fluorescence intensity and change in lifetimes were observed compared to the emission maximum, fluorescence intensity and life times of GSala. These observations strongly support the possibility that GSala undergoes a conformational change on binding with ligands and each ligand produced different conformational changes in GSala. Also, different concentrations of each ligand produced different protein conformations in the enzyme GSala.
dc.identifier.issn1314-6246
dc.identifier.urihttps://doi.uni-plovdiv.bg/handle/store/114
dc.language.isoen
dc.publisherPlovdiv University Press “Paisii Hilendarski”
dc.subjectglutamine synthetase
dc.subjectfluorescence spectroscopy
dc.subjectconformational changes
dc.titleFluorescence study on ligand induced conformational changes of glutamine synthetase from Bacillus brevis Bb G1 under sporulating conditions
dc.typeArticle
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