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Impact of chromate and dichromate on lysozyme stability: A spectroscopic and molecular docking investigation
S. Subadini, RS. Panigrahy, NK. Gupta, K. Bera, H. Sahoo
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články
Grantová podpora
GF20-05789 L
Czech Science Foundation
PubMed
35305059
DOI
10.1002/bio.4231
Knihovny.cz E-zdroje
- MeSH
- chromany * MeSH
- cirkulární dichroismus MeSH
- fluorescenční spektrometrie MeSH
- muramidasa * chemie MeSH
- simulace molekulového dockingu MeSH
- termodynamika MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- Publikační typ
- časopisecké články MeSH
A comparative study of interaction between chicken egg white lysozyme (Lyz) with two hexavalent chromate ions; chromate and dichromate; which are prevalently known for their toxicity, was investigated using different spectroscopic techniques along with a molecular docking study. Both steady-state and time-resolved studies revealed that the addition of chromate/dichromate is responsible for strong quenching of intrinsic fluorescence in Lyz and the quenching is caused by both static and dynamic quenching mechanisms. Different binding and thermodynamic parameters were also calculated at different temperatures from the intrinsic fluorescence of Lyz. The conformational change in Lyz and thermodynamic parameters obtained during the course of interaction with chromate/dichromate were well-supported by the molecular docking results.
Biophysical and Protein Chemistry Laboratory Department of Chemistry NIT Rourkela Rourkela India
CEITEC MU Masaryk University Brno Czech Republic
Center of Nanomaterials NIT Rourkela Rourkela India
Department of Science Roma Tre University Rome Italy
National Center for Biomolecular Research Faculty of Science Masaryk University Brno Czech Republic
Citace poskytuje Crossref.org
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- $a A comparative study of interaction between chicken egg white lysozyme (Lyz) with two hexavalent chromate ions; chromate and dichromate; which are prevalently known for their toxicity, was investigated using different spectroscopic techniques along with a molecular docking study. Both steady-state and time-resolved studies revealed that the addition of chromate/dichromate is responsible for strong quenching of intrinsic fluorescence in Lyz and the quenching is caused by both static and dynamic quenching mechanisms. Different binding and thermodynamic parameters were also calculated at different temperatures from the intrinsic fluorescence of Lyz. The conformational change in Lyz and thermodynamic parameters obtained during the course of interaction with chromate/dichromate were well-supported by the molecular docking results.
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