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Conformational features of disulfide intact and reduced forms of hen egg white lysozyme in aqueous solution in the presence of trifluoroethanol (TFE): Implications for protein folding intermediates

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Title Conformational features of disulfide intact and reduced forms of hen egg white lysozyme in aqueous solution in the presence of trifluoroethanol (TFE): Implications for protein folding intermediates
 
Creator RATNAPRABHA, C
SASIDHAR, YU
 
Subject molten globule state
secondary structure
beta-lactoglobulin
circular-dichroism
alpha-lactalbumin
propensity
bonds
nmr
 
Description The conformational features of reduced and disulfide intact hen egg white lysozyme in aqueous 2,2,2-trifluoroethanol (TFE) solutions have been examined using circular dichroism and fluorescence spectroscopies. We find that non-native like and molten globule like states are induced in reduced lysozyme, with non-native like and native like alpha helicities and with reduced accessibility of tryptophans to collisional quencher acrylamide, in the presence of TFE as judged from circular dichroism and fluorescence experiments. We correlate our results to kinetic hydrogen-deuterium exchange NMR results of the refolding of lysozyme available in the literature. We discuss the implications of our results for disulfide bond formation and protein folding intermediates.
 
Publisher ROYAL SOC CHEMISTRY
 
Date 2011-08-28T09:01:08Z
2011-12-26T12:57:58Z
2011-12-27T05:46:36Z
2011-08-28T09:01:08Z
2011-12-26T12:57:58Z
2011-12-27T05:46:36Z
1998
 
Type Article
 
Identifier JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS, 94(24), 3631-3637
0956-5000
http://dx.doi.org/10.1039/a806138f
http://dspace.library.iitb.ac.in/xmlui/handle/10054/11698
http://hdl.handle.net/10054/11698
 
Language en