volume 32, issue 44, P11886-11894 1993
DOI: 10.1021/bi00095a018
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Herman Van Dael, Petra Haezebrouck, Ludmilla Morozova, Christopher Arico-Muendel, Christopher M. Dobson

Abstract: Despite their homologous structure, c-type lysozymes and alpha-lactalbumins have been found to differ profoundly in their unfolding behavior, in that the alpha-lactalbumins readily enter a partially unfolded collapsed state (the "molten globule"), whereas lysozymes unfold cooperatively to a highly unfolded state. The calcium-binding property of lysozyme from equine milk provides an evolutionary link between the two families of proteins. We demonstrate here that equine lysozyme undergoes a two-stage unfolding t…

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