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• W2488893896 endingPage "2030" @default.
• W2488893896 startingPage "2016" @default.
• W2488893896 abstract "Herein, the binding of 1-methyl-3-octylimidazolium chloride [OMIM][Cl] ionic liquid with hen egg white lysozyme (HEWL) has been studied using fluorescence, time resolved fluorescence, UV–visible and circular dichroism (CD) spectroscopy, in combination with computational study. The fluorescence results revealed that [OMIM][Cl] quenches the fluorophore of HEWL through static quenching mechanism. The calculated thermodynamic parameters show that [OMIM][Cl] bind with HEWL through hydrophobic interactions. In addition, the negative value of Gibbs energy change (∆G) indicates that the binding process was spontaneous. Furthermore, UV–vis and CD results indicate that [OMIM][Cl] induce the conformational change in HEWL and increase its enzymatic activity. Additionally, molecular docking results showed that [OMIM][Cl] binds at the active site of HEWL where both the fluorophore residues (Trp108 and Trp62) and the catalytic residues (Glu35 and Asp52) reside. Molecular dynamic simulation results show the reduction of intra-molecular hydrogen bond of HEWL when it binds with [OMIM][Cl]." @default.
• W2488893896 created "2016-08-23" @default.
• W2488893896 creator A5016581055 @default.
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• W2488893896 creator A5039919375 @default.
• W2488893896 creator A5054678939 @default.
• W2488893896 creator A5055931280 @default.
• W2488893896 date "2016-08-05" @default.
• W2488893896 modified "2023-10-10" @default.
• W2488893896 title "Effect of 1-methyl-3-octyleimmidazolium chloride on the stability and activity of lysozyme: a spectroscopic and molecular dynamics studies" @default.
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• W2488893896 doi "https://doi.org/10.1080/07391102.2016.1204946" @default.
• W2488893896 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27426036" @default.
• W2488893896 hasPublicationYear "2016" @default.
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