Unfolding intermediate of a multidomain protein, calmodulin, in urea as revealed by small-angle X-ray scattering

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Abstract

The denaturation of calmodulin (CaM) induced by urea has been studied by small-angle X-ray scattering, which is a direct way to evaluate the shape changes in a protein molecule. In the absence of Ca2+, the radii of gyration (Rg) of CaM are 20.8±0.3 Å in the native state and about 34±1.0 Å in the unfolded state. The transition curve derived from Kratky plots indicates a bimodal transition via a stable unfolding intermediate around 2.5 M urea. In the presence of Ca2+ and in the presence of both Ca2+ and a target peptide, the Rg values are 21.5±0.3 and 18.1±0.3 Å in the native state and 26.7±0.4 and 24.9±0.4 Å at 9 M urea, respectively. The results indicate that a stable unfolding intermediate still persists in 9 M urea. The present results suggest that the shape of unfolding intermediates is an asymmetric dumbbell-like structure, one in the folded and one in the unfolded state. © 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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Yokouchi, T., Izumi, Y., Matsufuji, T., Jinbo, Y., & Yoshino, H. (2003). Unfolding intermediate of a multidomain protein, calmodulin, in urea as revealed by small-angle X-ray scattering. FEBS Letters, 551(1–3), 119–122. https://doi.org/10.1016/S0014-5793(03)00907-4

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