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Conformational features of reduced and disulfide intact forms of hen egg white lysozyme in aqueous solution in presence of 3-chloro-1, 2-propanediol and dioxane: Implications for protein folding intermediates

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Title Conformational features of reduced and disulfide intact forms of hen egg white lysozyme in aqueous solution in presence of 3-chloro-1, 2-propanediol and dioxane: Implications for protein folding intermediates
 
Creator SASIDHAR, YU
PRABHA, CR
 
Subject molten globule state
secondary structure
alpha-lactalbumin
trifluoroethanol
bonds
 
Description Conformational features of reduced and disulfide intact hen egg white lysozyme in aqueous 1,4-dioxane and 3-chloro-1, 2-propanediol solutions have been examined using circular dichroism and fluorescence spectroscopy. We find that in presence of 1, 4-dioxane, reduced lysozyme assumes a relatively compact conformational form with secondary structure closer to native state and no tertiary structure as judged by peptide and aromatic CD spectra and ANS binding studies monitored by fluorescence. Further, in presence of 40% (v/v) 3-chloro-1, 2-propanediol, disulfide intact lysozyme (DI-lysozyme) assumes a conformational form with native like secondary structure and no tertiary structure akin to a molten globule state. We correlate our results to kinetic hydrogen- deuterium exchange NMR results of the refolding of lysozyme available in literature and suggest that the conformational forms observed in our study could be models for kinetic intermediates in the refolding of lysozyme.
 
Publisher NATL INST SCIENCE COMMUNICATION
 
Date 2011-08-19T04:09:08Z
2011-12-26T12:56:03Z
2011-12-27T05:44:10Z
2011-08-19T04:09:08Z
2011-12-26T12:56:03Z
2011-12-27T05:44:10Z
2000
 
Type Article
 
Identifier INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS, 37(2), 97-106
0301-1208
http://dspace.library.iitb.ac.in/xmlui/handle/10054/10221
http://hdl.handle.net/10054/10221
 
Language en