絞り込み

17439

広告

Insight into Protein-Polymer Conjugate Relaxation Dynamics: The Importance of Polymer Grafting.

著者 Russo D , Pelosi C , Wurm FR , Frick B , Ollivier J , Teixeira J
Macromol Biosci.2020 Apr 13 ; ():e1900410.
この記事をPubMed上で見るPubMedで表示
この記事をGoogle翻訳上で見る Google翻訳で開く

スターを付ける スターを付ける     (1view , 0users)

Full Text Sources

Miscellaneous

Research Materials

The bio and chemical physics of protein-polymer conjugates are related to parameters that characterize each component. With this work, it is intended to feature the dynamical properties of the protein-polymer conjugate myoglobin (Mb)-poly(ethyl ethylene phosphate), in the ps and ns time scales, in order to understand the respective roles of the protein and of the polymer size in the dynamics of the conjugate. Elastic and quasi-elastic neutron scattering is performed on completely hydrogenated samples with variable number of polymer chains covalently attached to the protein. The role of the polymer length in the protein solvation and internal dynamics is investigated using two conjugates formed by polymers of different molecular weight. It is confirmed that the flexibility of the complex increases with the number of grafted polymer chains and that a sharp dynamical transition appears when either grafting density or polymer molecular weight are high. It is shown that protein size is crucial for the polymer structural organization and interaction on the protein surface and it is established that the glass properties of the polymer change upon conjugation. The results give a better insight of the equivalence of the polymer coating and the role of water on the surface of proteins.
PMID: 32285628 [PubMed - as supplied by publisher]
印刷用ページを開く Endnote用テキストダウンロード