To use all functions of this page, please activate cookies in your browser.
my.chemeurope.com
With an accout for my.chemeurope.com you can always see everything at a glance – and you can configure your own website and individual newsletter.
- My watch list
- My saved searches
- My saved topics
- My newsletter
Denaturation midpointAssuming two-state protein folding, denaturation midpoint is defined as that temperature (Tm) or denaturant concentration (Cm) at which both the folded and unfolded states are equally populated. Additional recommended knowledgeIf the widths of the folded and unfolded wells are assumed to be equal both these states will have identical free energies at the midpoint. However, for natural proteins this is not the case. There is an inherent asymmetry as evidenced by the difference in heat capacities between them - the folded ensemble has a lower heat capacity (in other words, lower fluctuations thus indicating a narrower well) than the unfolded ensemble. This would mean that the free energy of the folded state is lower at the denaturation midpoint than the unfolded state. In such a scenario, the temperature at which both the wells have identical free energies is termed the characteristic temperature (To).[1] References
|
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Denaturation_midpoint". A list of authors is available in Wikipedia. |