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Issue 6, 2012
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Hyper-thermal stability and unprecedented re-folding of solvent-free liquid myoglobin

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Abstract

Isolating solvent effects by studying proteins in a liquid phase devoid of solvent has not been previously possible because freeze-dried protein solids do not melt but thermally degrade. Herein we circumvent this problem by modifying the interactions between myoglobin molecules via a polymer-surfactant coronal layer to produce a solvent-free liquid phase that is thermally stable over a wide temperature range. Using high-resolution synchrotron radiation circular dichroism and UV-Vis spectroscopies we determine the temperature-dependent structure and re-folding behaviour of cationized myoglobin under solvent-free conditions, and show that dehydration and subsequent melting of the nanoconstruct has no significant effect on the protein secondary structure at room temperature. Significantly, the solvent-free liquid myoglobin molecules exhibit hyper-thermophilic behaviour and can be reversibly re-folded by cooling from 155 °C. We attribute the abnormally high thermal stability and persistence of protein folding to entropic contributions associated with macromolecular crowding and confinement, and propose that re-folding in the absence of a solvent shell is facilitated by the configurational flexibility and molecular interactivity of the polymer surfactant coronal layer.

Graphical abstract: Hyper-thermal stability and unprecedented re-folding of solvent-free liquid myoglobin

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Supplementary files

Article information


Submitted
02 Feb 2012
Accepted
19 Mar 2012
First published
20 Mar 2012

Chem. Sci., 2012,3, 1839-1846
Article type
Edge Article

Hyper-thermal stability and unprecedented re-folding of solvent-free liquid myoglobin

A. P. S. Brogan, G. Siligardi, R. Hussain, A. W. Perriman and S. Mann, Chem. Sci., 2012, 3, 1839
DOI: 10.1039/C2SC20143G

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