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• W2186794029 abstract "The molten globule state of hen egg-white lysozyme (HEWL) is the major intermediate of a protein folding. Chaperones prevent aggregation and precipitation of proteins under conditions of stress. The present study aims to investigate the conformational state of the hen egg-white lysozyme when it in forming a high molecular weight complex with β-cyclodextrin (β-CyD) as a molecular chaperone using UV spectroscopy, fluorescence spectrophotometery, circular dichroism (CD) spectropolarimetry, Iso thermal titration (ITC) as well as the measurement of viscosity and Stokes radius of protein. The results showed that β-CyD reduces and delays the aggregation of lysozyme and increases the ANS (8-anilino-1naphthalenesulfonic acid) fluorescence intensity of the spectra. Therefore, a hydrophobic interaction occurred between β-CyD and lysozyme. In the range of 204–250 nm CD spectra of lysozyme did not change at the presence of β-CyD in ellipticity relative to native lysozyme. Measuring Stokes radius of lysozyme in the presence and absence of β-CyD and comparing its value with denatured state showed that molten globule was an intermediate state in protein folding process." @default.
• W2186794029 created "2016-06-24" @default.
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• W2186794029 date "2014-01-01" @default.
• W2186794029 modified "2023-09-27" @default.
• W2186794029 title "INTERACTION OF B-CYCLODEXTRIN WITH MOLTEN GLOBULE STATE OF HEN EGG-WHITE LYSOZYME" @default.
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