Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance upgrade on Thursday 4th of May 2017 from 8.00am to 9.00am (BST).

During this time our websites will be offline temporarily. If you have any questions please use the feedback button on this page. We apologise for any inconvenience this might cause and thank you for your patience.

Issue 6, 2012
Previous Article Next Article

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

Author affiliations


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

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 02 Feb 2012, accepted on 19 Mar 2012 and first published on 20 Mar 2012

Article type: Edge Article
DOI: 10.1039/C2SC20143G
Citation: Chem. Sci., 2012,3, 1839-1846
  •   Request permissions

    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

Search articles by author