Protein relaxation dynamics as affected by biocompatible and biodegradable polymer solvation – part IIb.
In our first experiment, we investigate the dynamics of polymer-protein conjugates using new biodegradable and highly water soluble polymers with two different chain lengths in conjugation with Maltose Binding Protein (MBP). An important findings was that 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. In a further experiment (performed on November 2016) we investigated BSA-polymer conjugates at three degree of polymerization (molar ratios of attached polymer chains: BSA-PEEP 1:5, 1:10, 1:20) and in the dry and hydrated stated. 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. First we intend to perform measurement on completely deuterated MBP-polymer conjugated. Then we also wish to use a new type of conjugate with a different secondary structure ( Myoglobin-polymer) in order to confirm some last unattended observed results.
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RUSSO Daniela; Simone Capaccioli; KOZA Michael Marek; OLLIVIER Jacques; PELOSI Chiara; PISCHEDDA Vittoria; TEIXEIRA Jose and WURM Frederick. (2018). Protein relaxation dynamics as affected by biocompatible and biodegradable polymer solvation – part IIb.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-815
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