The effect of N-methylation on the thermodynamic and spectroscopic features of a peptide mimicking the active site of NiSOD enzyme

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dc.contributor.advisorLihi, Norbert
dc.contributor.authorKazhykarim, Nazira
dc.contributor.departmentDE--Természettudományi és Technológiai Kar--Kémiai Intézet
dc.date.accessioned2024-12-18T08:41:48Z
dc.date.available2024-12-18T08:41:48Z
dc.date.created2024-11-12
dc.description.abstractIn this thesis work, the thermodynamic and spectroscopic features together with SOD activity studies of N-methylated peptide mimicking the active site of NiSOD enzyme were studied. To gain insights into mechanism of NiSOD-assisted superoxide dismutation, particularly the role of N-terminal amine protons from histidine in stabilizing superoxide anion via H-bond formation, the terminal amino group was substituted with a methyl group. The results were compared with those observed for the wild-type fragment of NiSOD. This study demonstrates that although the N-methylated peptide mimicking the active site of NiSOD exhibits structural features similar to wt-NiSOD, it fails to retain catalytic activity, clearly suggesting that the terminal amino group is involved in the hydrogen-bond network surrounding the catalytic center.
dc.description.courseChemical Engineering
dc.description.degreeBSc/BA
dc.format.extent29
dc.identifier.urihttps://hdl.handle.net/2437/383846
dc.language.isoen
dc.rights.accessHozzáférhető a 2022 decemberi felsőoktatási törvénymódosítás értelmében.
dc.subjectNickel Superoxide Dismutase enzyme
dc.subjectMechanism of catalysis
dc.subjectN-methylation
dc.subjectSOD activity
dc.subject.dspaceChemistry
dc.titleThe effect of N-methylation on the thermodynamic and spectroscopic features of a peptide mimicking the active site of NiSOD enzyme
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