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Polymer conjugation can affect nanoscale protein fluctuations.

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In the present paper we address the effects of polymer conjugation on protein dynamical fluctuations on the ns timescale. We analyze the dynamical properties of proteins conjugated with polymer in order to better understand the relative importance of molecular mechanisms related to hydration water versus bio-compatible materials. Using neutron scattering spectroscopy we present the investigation of the dynamics of a new class of polymer-protein conjugates, i.e. protein conjugation with fully degradable and highly water-soluble polymethyl ethylene phosphonate.

The highlight of our work is presented in the experimental investigation performed with partially deuterated conjugates at two different polymer molecular weights . Here we describe for the first time that polymers do not promote a dynamical transition in absence of hydration water and that the length of the polymers within the conjugate is important for the degree of the protein flexibility in the dry and hydrated state. We discuss these findings in the context of protein environmental dynamics.
This study done in collaboration between researchers from Lyon, Grenoble, Perugia and Mainz has recently been highlighted on the cover of Biomacromolecules .