Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/14871
Title: Molecular mechanisms underlying the thermal stability and acid-induced unfolding of CHABII
Authors: WEI ZHENG
Keywords: protein folding; molten globule; CHABII; pH-induced unfolding; thermal stability; NMR spectroscopy
Issue Date: 10-Nov-2005
Source: WEI ZHENG (2005-11-10). Molecular mechanisms underlying the thermal stability and acid-induced unfolding of CHABII. ScholarBank@NUS Repository.
Abstract: CHABII was previously demonstrated to undergo a gradual pH-induced unfolding. CHABII at pH 4.0 offers an attractive model for deeper understanding of the molten globule state. In the present study, the recombinant proteins of CHABII and its mutant [Phe21]-CHABII were expressed and refolded. Extensive CD, NMR characterizations showed that replacement of His21 by Phe in [Phe21]-CHABII eliminated the pH-induced unfolding from pH 6.5 to 4.0 and considerably enhanced the packing interaction of the hydrophobic core, increasing the thermal stability of [Phe21]-CHABII by ~17 degrees. For CHABII at pH 4.0, the 1H-15N HSQC spectrum was poorly-dispersed while the persistence of medium- and long-range NOEs indicated its highly native-like topology, strongly implying that the degree of the native-like topology might be significantly underestimated in the previous characterization of partially-folded and even a??completely-unfoldeda?? proteins.
URI: http://scholarbank.nus.edu.sg/handle/10635/14871
Appears in Collections:Master's Theses (Open)

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
Master_Thesis_WZ3.pdf1.23 MBAdobe PDF

OPEN

NoneView/Download

Page view(s)

289
checked on Dec 11, 2017

Download(s)

171
checked on Dec 11, 2017

Google ScholarTM

Check


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