Are the molten globule and the unfolded states of apo-α-lactalbumin enthalpically equivalent?

Xie, Dong ; Bhakuni, Vinod ; Freire, Ernesto (1993) Are the molten globule and the unfolded states of apo-α-lactalbumin enthalpically equivalent? Journal of Molecular Biology, 232 (1). pp. 5-8. ISSN 0022-2836

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00222...

Related URL: http://dx.doi.org/10.1006/jmbi.1993.1364

Abstract

Recently, the absence of a thermally induced transition has been offered as proof that the unfolded and the molten globule states of apo-α-lactalbumin are enthalpically equivalent. In this paper we demonstrate that that argument is thermodynamically incorrect. In addition, it is shown that the absence of a thermally induced transition at extremely low salt concentrations can be accounted for in terms of the known ionic strength dependence of the transition temperature and the thermodynamic parameters associated with the unfolding of apo-α-lactalbumin.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Apo-α-lactalbumin; Molten Globule; Protein Folding; Thermodynamics; Calorimetry
ID Code:20935
Deposited On:20 Nov 2010 13:18
Last Modified:17 Jan 2011 12:05

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