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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, Y U
Prabha, C Ratna
 
Description 97-106
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.
 
Date 2013-07-16T07:06:25Z
2013-07-16T07:06:25Z
2000-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/19816
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.37(2) [April 2000]