Laboratoire Léon Brillouin
UMR12 CEA-CNRS, Bât. 563 CEA Saclay
91191 Gif sur Yvette Cedex, France
+33-169085241 llb-sec@cea.fr
D. Russo, A. De Angelis, A. Paciaroni, B. Frick, N. de Sousa, F. R. Wurm, and J. Teixeira
We investigate the relaxation dynamics of protein−polymer conjugates by neutron scattering spectroscopy to understand to which extent the coating of a protein by a polymer can replace water in promoting thermal structural fluctuations. For this purpose, we compare the dynamics of protein−polymer mixtures to that of conjugates with a variable number of polymers covalently attached to the protein. Results show that the flexibility of the protein is larger in protein−polymer mixtures than in native protein or in conjugates, even in the dry state. Upon hydration, both the native protein and the conjugate show equivalent dynamics, suggesting that the polymer grafted on the protein surface adsorbs all water molecules.
• Physique et chimie pour le vivant et l’environnement › Physique et vivant / Physics and life › Biophysique › Matière Molle
Physics and chemistry for life sciences and the environment
• Laboratoire Léon Brillouin (LLB) • Leon Brillouin Laboratory (LLB)
• Biologie et Systèmes Désordonnés - GBSD (appareils 7C2, Paxe, Mibemol et Muse) • Disordered System and Biology - GSDB
• Neutrons • Le quasi-élastique • Neutrons • Quasi-elastic scattering