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

• Autorzy: Iloro I. , Goni F.M. , Arrondo J.L.R.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

urea-induced denaturation; heat-induced denaturation; two-dimensional infrared correlation spectroscopy; sarcoplasmic reticulum; infrared spectroscopy

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2005
• Tom: 52
• Numer: 2
• Opis fizyczny: p.477-483,fig.,ref.

Twórcy

autor

Iloro I.

• Universidad del Pais Vasco, Bilbao, Spain

autor

Goni F.M.

autor

Arrondo J.L.R.

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