Protein relaxation dynamics as affected by biocompatible and biodegradable polymer solvation - part II.
Protein-polymer conjugates combine the biological activities of proteins with the convenient handling and processability of synthetic polymers, and was proven to be an efficient strategy to improve biotechnologies based on protein such as drug delivery. In our first previous experiment, we investigate the dynamics of polymer-protein conjugates using new biodegradable and highly water soluble polymers in conjugation with Maltose binding protein. We were able to show that polymer solvation, in the absence of water, enhances protein fluctuations, but does not enable the protein to undergo the dynamical transition as previously observed in native proteins or in solvent-free liquid proteins. We also observe that the polymer loses its glass properties, providing a signature of a reciprocal and complex influence of both components on their respective dynamics. In this continuation proposal, we aim to better understand the enhancement of protein flexibility and what is the role of hydration water in the (conjugated) protein dynamics. We wish to highlight why the vitreous properties of the polymer are absent in the conjugates and in which conditions they can be re-established
Please note that you will need to login with your ILL credentials to download the data.
Download DataThe recommended format for citing this dataset in a research publication is in the following format:
RUSSO Daniela; DE ANGELIS Andrea; Bernhard Frick; OLLIVIER Jacques; PLAZANET Marie; TEIXEIRA Jose and WURM Frederick. (2016). Protein relaxation dynamics as affected by biocompatible and biodegradable polymer solvation - part II.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-778
ILL has partnered with DataCite as the registration agency
for data persistent identifiers.