Home

About

Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network
FAQHELPSITE MAPCONTACT US


  Advanced Search  

 
"Control of protein folding and misfolding in ionic liquid media, and a conjecture on early earth biology".
 

Summary: "Control of protein folding and misfolding in ionic liquid media, and a
conjecture on early earth biology".
C. Austen Angell
Dept. of Chemistry and Biochemistry, Arizona State University. Tempe, AZ
We describe recent studies [1-4] in which many of the complex features of biomolecule
behavior, such as protein folding and fibrillization, are reproduced (with little change
from biological behavior) in hydrated (10-20 wt % water) protic ionic liquid solutions
(PILs) in which the water activity is only a small fraction of its normal value. An
outstanding finding of these studies has been the stabilization against the normal
deteriorating influences of aggregation and hydrolysis, of model proteins like lysozyme
and ribonuclease A, when in the PILs environment. To characterize the protein stability
we define a "refoldability", or "refolding index" (RFI), which is the percentage of a
protein that refolds after an unfolding scan conducted in a differential scanning
calorimeter at 20K/min, followed by intrument cooling. This percentage is determined by
comparison of first and second unfolding endotherms, RFI =100Hd2/Hd1 and, for the
above proteins in their stable zones, is 97-99.
We then show how the proton activity in the (H3O+
-free) PIL can be characterized
by the NMR chemical shift of the lone proton on a PIL cation, such as diethylmethyl-
ammonium, (N-H). This varies greatly as the anion is changed from acetate to

  

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

 

Collections: Materials Science; Chemistry