Monitoring Protein Unfolding and DNA binding using Protein Charge Transfer Spectra

dc.contributor.authorPriyadarshi, Anurag
dc.date.accessioned2024-12-09T09:59:04Z
dc.date.available2024-12-09T09:59:04Z
dc.date.issued2023
dc.descriptionSupervisor: Swaminathan, Rajaram
dc.description.abstractProteins are not expected to show electronic absorption or emission in the near UV-Visible region in the absence of aromatic amino acid residues and cofactors. However, evidence of novel protein absorbance and luminescence in the near UV-Visible region independent of the presence of aromatic amino acid residues has now been presented by multiple research groups. By employing Time-dependent density-functional theory (TDDFT) calculations, it was postulated that charge transfer involving charged atoms in the Lys/Glu sidechain and the peptide backbone gave rise to the novel absorbance observed in the 250—800 nm region for protein α3C. This previously unknown intrinsic chromophore was termed Protein Charge Transfer Spectra (ProCharTS) by Prasad et al. Characteristic features of the observed blue luminescence include low to moderate quantum yields, excitation-emission spectral overlap among the multiple proteins studied, large Stokes shifts, and similar mean lifetimes for luminescence intensity decays.
dc.identifier.otherROLL NO.156106026
dc.identifier.urihttps://gyan.iitg.ac.in/handle/123456789/2713
dc.language.isoen
dc.relation.ispartofseriesTH-3036
dc.titleMonitoring Protein Unfolding and DNA binding using Protein Charge Transfer Spectra
dc.typeThesis
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