Protein – Metal ion Interaction: A Spectroscopic Study

Author(s)	DIVYA LAKSHMI TV, USHA K. ARAVIND
Country	India
Abstract	This study reports on the spectroscopic interaction studies of mercuric chloride LYZ. The quencher concentration was maintained in the range of 0–6.25 µM. At the studied concentration range (10-6 M), LYZ did not have any variation in fluorescence intensity. Increase in LYZ concentration to 10-3 M showed a decrease in the fluorescence intensity due to the involvement of nucleophilic functional group. The fluorescence of LYZ was quenched to a large extent depending on the protein solution pH (2.2, 4.5, and 7.4).At all the studied pH, emission spectra showed blue shift. The onset and the shift varied with solution pH. Stern-Volmer analysis showed a three stage transition At pH 7.4, the presence of HgCl2 did not have much influence on the amide bands. But at pH 4.5, the amide I band showed a shift to lower wavenumber These confirmed that the quenching takes place through both static and energy transfer processes.
Keywords	Protein-Metal ion interaction, LYZ- Lysozyme, CHI-Chitosan, S-V- Stern Volmer Plot, FL- Fluorescence Intensity
Field	Chemistry
Published In	Volume 5, Issue 5, September-October 2023
Published On	2023-10-17
Cite This	Protein – Metal ion Interaction: A Spectroscopic Study - DIVYA LAKSHMI TV, USHA K. ARAVIND - IJFMR Volume 5, Issue 5, September-October 2023. DOI 10.36948/ijfmr.2023.v05i05.7679
DOI	https://doi.org/10.36948/ijfmr.2023.v05i05.7679
Short DOI	https://doi.org/gswg59

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