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

Ibón Iloro; Félix M Goñi; José L R Arrondo

doi:10.18388/abp.2005_3462

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

Ibón Iloro Unidad de Biofísica (Centro Mixto CSIC-UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Bilbao, Spain.;
Félix M Goñi
José L R Arrondo

DOI: https://doi.org/10.18388/abp.2005_3462

Abstract

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 approximately 45 degrees 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.

Published

2005-06-25

Issue

Vol. 52 No. 2 (2005)

Section

Articles

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