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Arakawa, T., Bhat, R. and Timasheff, S.N. (1990) Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry, 29, 1924- 1931. doi:10.1021/bi00459a037

has been cited by the following article:

  • TITLE: Thermal stability of proteins in the presence of aprotic ionic liquids

    AUTHORS: Hidetaka Noritomi, Ken Minamisawa, Reo Kamiya, Satoru Kato

    KEYWORDS: Thermal Stability; Lysozyme; Ionic Liquid; Remaining Activity

    JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.4 No.2, February 25, 2011

    ABSTRACT: Thermal stability of lysozyme dissolved in aqueous solutions was examined in the presence of water-miscible aprotic ionic liquids consisting of 1-ethyl-3-methylimidazolium cation and several kinds of anions. Addition of ionic liquids to an aqueous solution containing lysozyme prevented unfolded proteins from aggregating irreversibly at high temperatures. The thermal denaturation curve of lysozyme with ionic liquids was entirely shifted to higher temperature, compared with that without ionic liquids. The remaining activity of lysozyme after the heat treatment was markedly dependent upon the kind and concentration of ionic liquids. The remaining activi-ties of lysozyme with 1.5 M 1-ethyl-3-methylimida-zolium tetrafluoroborate ([emim][BF4]) and 0.1 M 1-ethyl-3-methylimidazolium trifluoromethanesulfonate ([emim][Tf]) exhibited 88 and 68% after the heat treatment at 90oC for 30 min, respectively, although that without ionic liquids was perfectly lost.