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The "refoldability" of selected proteins in ionic liquids as a stabilization criterion, leading to a conjecture on biogenesis.
 

Summary: The "refoldability" of selected proteins in ionic liquids as a stabilization criterion,
leading to a conjecture on biogenesis.
Nolene Byrne, Jean-Philippe Belieres and C. Austen Angell, Dept. of Chemistry and
Biochemistry Arizona State University, Tempe, AZ
The folding of proteins is usually studied in dilute aqueous solutions of controlled pH, but it has
recently been demonstrated that reversible unfolding can occur in other media. Particular
stability is conferred on the protein (folded or unfolded) when the process occurs in "protic ionic
liquids" (pILs) of controlled proton activity (PA). This activity ("effective pH") is determined by
the acid and base components of the pIL and is characterized in this study by the proton chemical
shift of the N-H proton. Here we propose a "refoldability" or "refolding index" (RFI) metric for
assessing the stability of folded biomolecules in different solvent media, and demarcate high RFI
zones in hydrated pIL media using ribonuclease A (Rnase A) and hen egg white lysozyme
(HWL) as examples. Then we show that, unexpectedly, the same high RFIs can be obtained in
pIL media that are 90 % inorganic in character (simple ammonium salts). This leads us to a
conjecture related to the objections that have been raised to "primordial soup" theories for
biogenesis, objections that are based on the observation that all the bonds involved in
biomacromolecule formation are hydrolysed in ordinary aqueous solutions unless specifically
protected. The ingredients for primitive ionic liquids (NH3, CO, HCN, CO2 and water were
abundant in early earth atmosphere, and many experiments have shown how aminoacids could
form from them also. Cyclical concentration in evaporating inland seas could easily produce the

  

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

 

Collections: Materials Science; Chemistry