DSpace
 

DSpace at IIT Bombay >
IITB Publications >
Article >

Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/11698

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
Authors: RATNAPRABHA, C
SASIDHAR, YU
Keywords: molten globule state
secondary structure
beta-lactoglobulin
circular-dichroism
alpha-lactalbumin
propensity
bonds
nmr
Issue Date: 1998
Publisher: ROYAL SOC CHEMISTRY
Citation: JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS, 94(24), 3631-3637
Abstract: 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.
URI: http://dx.doi.org/10.1039/a806138f
http://dspace.library.iitb.ac.in/xmlui/handle/10054/11698
http://hdl.handle.net/10054/11698
ISSN: 0956-5000
Appears in Collections:Article

Files in This Item:

There are no files associated with this item.

View Statistics

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Valid XHTML 1.0! DSpace Software Copyright © 2002-2010  Duraspace - Feedback