The interaction between proteins and hydration water stabilizes protein structure and promotes functional dynamics, with water translational motions enabling protein flexibility. Engineered solvent-free protein-polymer hybrids have been shown to preserve protein structure, function, and dynamics. Here, we used neutron scattering, protein and polymer perdeuteration, and molecular dynamics simulations to explore how a polymer dynamically replaces water. Even though relaxation rates and vibrational properties are strongly modified in polymer coated compared to hydrated proteins, liquidlike polymer dynamics appear to plasticize the conjugated protein in a qualitatively similar way as do hydration-water translational motions.
Bibliographical noteFunding Information:
We are indebted to Laurent Heux for the use of calorimeter at CERMAV (Grenoble) and Pierre Sailler for the assistance during the calorimetry experiment. We thank Matthias Heyden for providing his custom-made trajectory analysis software. Financial support by the CEA, the CNRS, and the U. G. A. is acknowledged, as well as a grant from the Agence Nationale de la Recherche (Project No. ANR-11-BSV5-027) to M. W. The I. B. S. acknowledges integration into the Interdisciplinary Research Institute of Grenoble (IRIG, CEA). This work used the platforms of the Grenoble Instruct-ERIC center (ISBG ; UMS 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). This project has received funding from the European Union’s 7th Framework Programme for research, technological development and demonstration under the NMI3-II Grant No. 283883. We thank the UKRI for support for AWP (MR/S016430/1 and EP/K026720/1).
© 2021 American Physical Society.