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dc.contributor.authorKundu, Partha P.
dc.contributor.authorBhowmick, Tuhin
dc.contributor.authorSwapna, Ganduri
dc.contributor.authorKumar, G. V. Pavan
dc.contributor.authorNagaraja, V.
dc.contributor.authorNarayana, Chandrabhas
dc.identifier.citationKundu, PP; Bhowmick, T; Swapna, G; Kumar, GVP; Nagaraja, V; Narayana, C, Allosteric Transition Induced by Mg2+ Ion in a Transactivator Monitored by SERS. Journal of Physical Chemistry B 2014, 118 (20) 5322-5330,
dc.identifier.citationJournal of Physical Chemistry Ben_US
dc.descriptionRestricted Accessen_US
dc.description.abstractWe demonstrate the utility of the surface-enhanced Raman spectroscopy (SERS) to monitor conformational transitions in protein upon ligand binding. The changes in protein's secondary and tertiary structures were monitored using amide and aliphatic/aromatic side chain vibrations. Changes in these bands are suggestive of the stabilization of the secondary and tertiary structure of transcription activator protein C in the presence of Mg2+ ion, whereas the spectral fingerprint remained unaltered in the case of a mutant protein, defective in Mg2+ binding. The importance of the acidic residues in Mg2+ binding, which triggers an overall allosteric transition in the protein, is visualized in the molecular model. The present study thus opens up avenues toward the application of SERS as a potential tool for gaining structural insights into the changes occurring during conformational transitions in proteins.en_US
dc.publisherAmerican Chemical Societyen_US
dc.rights@American Chemical Society, 2014en_US
dc.subjectPhysical Chemistryen_US
dc.subjectSurface-Enhanced Ramanen_US
dc.subjectLabel-Free Detectionen_US
dc.subjectMu C-Proteinen_US
dc.subjectSecondary Structureen_US
dc.subjectSilver Electrodeen_US
dc.subjectColloidal Silveren_US
dc.titleAllosteric Transition Induced by Mg2+ Ion in a Transactivator Monitored by SERSen_US
Appears in Collections:Research Articles (Chandrabhas N.)
Research Articles (Nagaraja, V.)

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