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

• Authors: Ibón Iloro , Félix M Goñi , José L R Arrondo
• Languages of publication: EN

Abstracts

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.

Keywords

EN

2D-IR; urea-induced denaturation; sarcoplasmic reticulum; heat-induced denaturation

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2005
• Volume: 52
• Issue: 2
• Pages: 477-483

Dates

published

2005

received

2005-05-10

accepted

2005-05-13

revised

2005-05-13

Contributors

author

Ibón Iloro

• Unidad de Biofísica (Centro Mixto CSIC-UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Bilbao, Spain

author

Félix M Goñi

• Unidad de Biofísica (Centro Mixto CSIC-UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Bilbao, Spain

author

José L R Arrondo

• Unidad de Biofísica (Centro Mixto CSIC-UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Bilbao, Spain

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