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A 2D-IR study of heat- and [13C]urea-induced denaturation of sarcoplasmic reticulum Ca2+-ATPase.

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Iloro I., Goñi F. M., Arrondo J. L. R.
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2005
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vol. 52
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issue 2
477-483
EN
Two-dimensional infrared correlation spectroscopy (2D-IR) was applied to the study of urea- and heat-induced unfolding denaturation of sarcoplasmic reticulum Ca^(2+)-ATPase (SR ATPase). Urea at 2-3 M causes reversible loss of SR ATPase activity, while higher concentrations induce irreversible denaturation. Heat-induced denaturation is a non-two-state process, with an "intermediate state" (at t ≈ 45°C) characterized by the presence of protein monomers, instead of the native oligomers. 2D-IR reveals that urea denaturation causes loss of the structural transition to the "intermediate state". Whenever the urea effect can be reversed, the transition to the "intermediate state" is re-established.
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