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A 2D-IR study of heat- and [13 C]urea-induced denaturation of sarcoplasmic reticulum Ca2plus -ATPase

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Iloro I., Goni F. M., Arrondo J. L. R.

Acta Biochimica Polonica

2005

tom 52

nr 2

Two-dimensional infrared correlation spectroscopy (2D-IR) was applied to the study of urea- and heat-induced unfolding denaturation of sarcoplasmic reticulum Ca2+-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 ≈ 45oC) 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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Arrondo J. L. R.

1 Goni F. M.

1 Iloro I.

1 2005

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A 2D-IR study of heat- and [13 C]urea-induced denaturation of sarcoplasmic reticulum Ca2plus -ATPase