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Allosteric Transition Induced by Mg2+ Ion in a Transactivator Monitored by SERS

Kundu, Partha P and Bhowmick, Tuhin and Swapna, Ganduri and Kumar, Pavan GV and Nagaraja, Valakunja and Narayana, Chandrabhas (2014) Allosteric Transition Induced by Mg2+ Ion in a Transactivator Monitored by SERS. In: JOURNAL OF PHYSICAL CHEMISTRY B, 118 (20). pp. 5322-5330.

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Official URL: http://dx.doi.org/10.1021/jp5000733


We 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.

Item Type: Journal Article
Additional Information: copyright for this article belongs to AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Division of Physical & Mathematical Sciences > Physics
Date Deposited: 24 Jun 2014 05:57
Last Modified: 24 Jun 2014 07:41
URI: http://eprints.iisc.ac.in/id/eprint/49299

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