title: Temperature and solvent dependence of the dynamical landscape of tau protein conformations.
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.
authors.affiliation: Physics Department, Sapienza University of Rome, Piazzale A. Moro 2, 00185 Roma, Italy.
authors.forename: Antonio
authors.initials: A
authors.lastname: Bianconi
authors.forename: Gabriele
authors.initials: G
authors.lastname: Ciasca
authors.forename: Alexander
authors.initials: A
authors.lastname: Tenenbaum
authors.forename: Anna
authors.initials: A
authors.lastname: Battisti
authors.forename: Gaetano
authors.initials: G
authors.lastname: Campi
keywords: Intrinsic disordered proteins; Protein conformations; Temperature effects in protein fluctuations; Water effect in conformational landscape