You are not logged in.

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

Byrne, Nolene, Belieres, Jean-Philippe and Austen Angell, C. 2009, The "refoldability" of selected proteins in ionic liquids as a stabilization criterion, leading to a conjecture on biogenesis, Australian journal of chemistry, vol. 62, no. 4, pp. 328-333, doi: 10.1071/CH08441.

Attached Files
Name Description MIMEType Size Downloads

Title The "refoldability" of selected proteins in ionic liquids as a stabilization criterion, leading to a conjecture on biogenesis
Author(s) Byrne, Nolene
Belieres, Jean-Philippe
Austen Angell, C.
Journal name Australian journal of chemistry
Volume number 62
Issue number 4
Start page 328
End page 333
Total pages 6
Publisher CSIRO Publishing
Place of publication Collingwood, Vic
Publication date 2009-04-24
ISSN 0004-9425
1445-0038
Summary 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. This activity (‘effective pH’) is determined by the acid and base components of the pIL and is characterized in the present 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 and hen egg white lysozyme 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 hydrolyzed in ordinary aqueous solutions unless specifically protected. The ingredients for primitive ionic liquids (NH3, CO, HCN, CO2, and water) were abundant in the early earth atmosphere, and many experiments have shown how amino acids could form from them also. Cyclical concentration in evaporating inland seas could easily produce the type of ambient-temperature, non-hydrolyzing, media that we have demonstrated here may be hospitable to biomolecules, and that may be actually encouraging of biopolymer assembly. Thus a plausible variant of the conventional ‘primordial soup’ model of biogenesis is suggested.
Notes Special Issue: 3rd Australian Symposium
Language eng
DOI 10.1071/CH08441
Field of Research 039999 Chemical Sciences not elsewhere classified
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2009 CSIRO Publishing
Persistent URL http://hdl.handle.net/10536/DRO/DU:30039451

Document type: Journal Article
Collection: Centre for Material and Fibre Innovation
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 13 times in TR Web of Science
Scopus Citation Count Cited 13 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 263 Abstract Views, 1 File Downloads  -  Detailed Statistics
Created: Wed, 26 Oct 2011, 09:02:17 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.