Please use this identifier to cite or link to this item: http://lib.jncasr.ac.in:8080/jspui/handle/10572/2596
Title: Allosteric Transition Induced by Mg2+ Ion in a Transactivator Monitored by SERS
Authors: Kundu, Partha P.
Bhowmick, Tuhin
Swapna, Ganduri
Kumar, G. V. Pavan
Nagaraja, V.
Narayana, Chandrabhas
Keywords: Physical Chemistry
Surface-Enhanced Raman
Label-Free Detection
Mu C-Protein
Conformational-Changes
Bacteriophage-Mu
Single-Molecule
Amino-Acids
Secondary Structure
Silver Electrode
Colloidal Silver
Issue Date: 2014
Publisher: American Chemical Society
Citation: Kundu, 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, http://dx.doi.org/10.1021/jp5000733
Journal of Physical Chemistry B
118
20
Abstract: 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.
Description: Restricted Access
URI: http://hdl.handle.net/10572/2596
ISSN: 1520-6106
Appears in Collections:Research Articles (Chandrabhas N.)
Research Articles (Nagaraja, V.)

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