Summary: Reversible folding­unfolding, aggregation protection, and multi-year
stabilization, in high concentration protein solutions, using ionic liquids
Nolene Byrne, Li-Min Wang, Jean-Philippe Belieres and C. Austen Angell*
Received (in Cambridge, UK) 2nd January 2007, Accepted 30th March 2007
First published as an Advance Article on the web 19th April 2007
DOI: 10.1039/b618943a
We report the reversible thermal unfolding/refolding, and
long period stabilization against aggregation and hydrolysis,
of .200 mg ml21
solutions of lysozyme in ionic liquid-rich, ice-
avoiding, solvents.
Studies of protein folding are normally carried out in buffered
dilute aqueous solutions to avoid loss of protein to the aggregation
phenomenon. In a trial study three years ago1
we reported the
observation of refolding of lysozyme, after denaturation, in
samples of concentration up to 200 mg ml21
. It must be regarded
as remarkable that at this concentration not only was refolding
observed, but that the process could be repeated many times with

Source: Angell, C. Austen - Department of Chemistry and Biochemistry, Arizona State University

Collections: Materials Science; Chemistry