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Protein Unfolding, and the "Tuning In" of Reversible Intermediate States, in Protic Ionic Liquid Media
 

Summary: Protein Unfolding, and the "Tuning In" of Reversible
Intermediate States, in Protic Ionic Liquid Media
N. Byrne and C.A Angell
Department of Chemistry and
Biochemistry, Arizona State
University, Tempe,
AZ 85281-1604, USA
Received 21 November 2007;
received in revised form
16 February 2008;
accepted 25 February 2008
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. Previously, we have shown that solution of proteins in ionic-
liquid-rich solutions conveys surprising stabilization against hydrolysis and
aggregation, permitting multiple unfold/refold cycles without loss to aggre-
gation. Here, we show that the denaturing temperatures of both hen egg

  

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

 

Collections: Materials Science; Chemistry