Alfano, C;
Sanfelice, D;
Martin, SR;
Pastore, A;
Temussi, PA;
(2017)
An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states.
Nature Communications
, 8
, Article 15428. 10.1038/ncomms15428.
Preview |
Text
Sanfelice_an optimized_protein.pdf - Published Version Download (1MB) | Preview |
Abstract
Macromolecular crowding ought to stabilize folded forms of proteins, through an excluded volume effect. This explanation has been questioned and observed effects attributed to weak interactions with other cell components. Here we show conclusively that protein stability is affected by volume exclusion and that the effect is more pronounced when the crowder's size is closer to that of the protein under study. Accurate evaluation of the volume exclusion effect is made possible by the choice of yeast frataxin, a protein that undergoes cold denaturation above zero degrees, because the unfolded form at low temperature is more expanded than the corresponding one at high temperature. To achieve optimum sensitivity to changes in stability we introduce an empirical parameter derived from the stability curve. The large effect of PEG 20 on cold denaturation can be explained by a change in water activity, according to Privalov's interpretation of cold denaturation.
| Type: | Article |
|---|---|
| Title: | An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states |
| Location: | England |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1038/ncomms15428 |
| Publisher version: | http://doi.org/10.1038/ncomms15428 |
| Language: | English |
| Additional information: | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
| Keywords: | Proteins, Thermodynamics |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences |
| URI: | https://discovery.ucl.ac.uk/id/eprint/1557776 |
Archive Staff Only
 |
View Item |
