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dc.titleMolecular mechanisms underlying the thermal stability and acid-induced unfolding of CHABII
dc.contributor.authorWEI ZHENG
dc.identifier.citationWEI ZHENG (2005-11-10). Molecular mechanisms underlying the thermal stability and acid-induced unfolding of CHABII. ScholarBank@NUS Repository.
dc.description.abstractCHABII 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.
dc.subjectprotein folding; molten globule; CHABII; pH-induced unfolding; thermal stability; NMR spectroscopy
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.supervisorSONG JIANXING
dc.description.degreeconferredMASTER OF SCIENCE
Appears in Collections:Master's Theses (Open)

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