Unfolding of apomyoglobin from Aplysia limacina: the effect of salt and pH on the cooperativity of folding

Journal of Molecular Biology
R A StaniforthM Brunori

Abstract

The equilibrium unfolding pathway of Aplysia apomyoglobin has been studied under various solvent conditions. The protein exhibits a single unfolding transition in acid in contrast to the two transitions observed for the mammalian apomyoglobins with which it shares a common fold but a low level of sequence identity (24%). This acid-unfolded species has considerable residual structure as evidenced by both tryptophan fluorescence and far-UV CD spectroscopy. It remains 40% alpha-helical under low salt conditions (2 mM citrate, 4 degrees C); the folded form is 65% helical. A similar species is observed for the mammalian globins in mild acid conditions. Titration with GdnHCl at pH 7 reveals two unfolding transitions, the first having common features with that observed in acid and the second resulting in a completely unfolded state. Under the same conditions, urea unfolds the protein completely in an apparently single cooperative transition. Assuming a simple three-state model (F<-->I<-->U), data from GdnHCl and urea titrations over a range of pH conditions were used to derive values for the apparent stability (delta Gw(app) and solvent accessibility (n(app)) of the folded (F) and intermediate (I) forms of the protein. Urea titrations...Continue Reading

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Citations

Mar 5, 2016·Hepatitis Research and Treatment·Alexsandro S GaldinoFernando A G Torres
Dec 14, 2017·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Deborah K ShoemarkMaria Giulia Bigotti
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Mar 17, 2010·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Jianshuai MuXiangshi Tan

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