| Literature DB >> 23361965 |
Takahiro Muraoka1, Kota Adachi, Mihoko Ui, Shunichi Kawasaki, Nabanita Sadhukhan, Haruki Obara, Hidehito Tochio, Masahiro Shirakawa, Kazushi Kinbara.
Abstract
Part of the solution: A PEG with a discrete triangular structure exhibits hydrophilicity/hydrophobicity switching upon increasing temperatures, and suppresses the thermal aggregation of lysozyme to retain nearly 80 % of the enzymatic activity. CD and NMR spectroscopic studies revealed that, with the structured PEG, the higher-order structures of lysozyme persist at high temperature, and the native conformation is recovered after cooling.Entities:
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Year: 2013 PMID: 23361965 DOI: 10.1002/anie.201206563
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336