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Temperature and solvent dependence of the dynamical landscape of tau protein conformations

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Abstract

We report the variation with temperature of the ensemble distribution of conformations spanned by the tau protein in its dynamical states measured by small-angle X-ray scattering (SAXS) using synchrotron radiation. The SAXS data show a clear temperature variation of the distribution of occupied protein conformations from 293 to 318 K. More conformations with a smaller radius of gyration are occupied at higher temperature. The protein–solvent interactions are shown by computer simulation to be essential for controlling the dynamics of protein conformations, providing evidence for the key role of water solvent in the protein dynamics, as proposed by Giorgio Careri.

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Authors and Affiliations

  1. Physics Department, Sapienza University of Rome, Piazzale A. Moro 2, 00185, Roma, Italy

    Antonio Bianconi, Gabriele Ciasca & Alexander Tenenbaum

  2. Physics Department, University of Trento, Via Sommarive 14, 38123, Povo (Trento), Italy

    Anna Battisti

  3. LISC, FBK-CMM and University of Trento, Via Sommarive 18, 38123, Povo (Trento), Italy

    Anna Battisti

  4. CNR, Institute of Crystallography, Via Salaria Km 29.300, 00016, Monterotondo (Roma), Italy

    Gaetano Campi

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  1. Antonio Bianconi
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Correspondence to Antonio Bianconi.

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Bianconi, A., Ciasca, G., Tenenbaum, A. et al. Temperature and solvent dependence of the dynamical landscape of tau protein conformations. J Biol Phys 38, 169–179 (2012). https://doi.org/10.1007/s10867-011-9244-6

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