Reversible folding-unfolding, aggregation protection, and multi-year stabilization, in high concentration protein solutions, using ionic liquids.
نویسندگان
چکیده
We report the reversible thermal unfolding/refolding, and long period stabilization against aggregation and hydrolysis, of >200 mg ml(-1) solutions of lysozyme in ionic liquid-rich, ice-avoiding, solvents.
منابع مشابه
Protein unfolding, and the "tuning in" of reversible intermediate states, in protic ionic liquid media.
Protic ionic liquids (PILs) are currently being shown to be as interesting and valuable to chemical manipulations as the well-known aprotic ionic liquids (APIL). PILs have the additional advantage that the proton activity (PA) can be adjusted by the choice of Bronsted base and Bronsted acid used in their formation. In the absence of solvent, the PA plays the role of pH in ordinary solutions. Pr...
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متن کاملReversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle x-ray scattering.
To clarify mechanisms of folding and unfolding of proteins, many studies of thermal denaturation of proteins have been carried out at low protein concentrations because in many cases thermal denaturation accompanies a great tendency of aggregation. As small-angle x-ray scattering (SAXS) measurements are liable to use low-concentration solutions of proteins to avoid aggregation, SAXS has been re...
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عنوان ژورنال:
- Chemical communications
دوره 26 شماره
صفحات -
تاریخ انتشار 2007