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. 2014 Mar 18;4(1):354–373. doi: 10.3390/biom4010354

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© 2014 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Dependence of the protein folding equilibrium on temperature and the presence of denaturants. (A) Temperatures modify _N→U reaching a maximum value which corresponds to the maximal protein stability. Heating or cooling the sample will lead to a decrease in _N→U which will equal zero at the temperature of cold unfolding (T_c) and at the melting temperature (T_m). At both temperatures half the protein population is folded and the other half is unfolded; (B) Protein stability decrease following a linear function of the concentration of the chaotropic agent. _N→U reaches the zero value at the mid-denaturant concentration (C_m) where 50% of the population is folded and the other 50% is unfolded.

Inline graphic — Dependence of the protein folding equilibrium on temperature and the presence of denaturants. (A) Temperatures modify _N→U reaching a maximum value which corresponds to the maximal protein stability. Heating or cooling the sample will lead to a decrease in _N→U which will equal zero at the temperature of cold unfolding (T_c) and at the melting temperature (T_m). At both temperatures half the protein population is folded and the other half is unfolded; (B) Protein stability decrease following a linear function of the concentration of the chaotropic agent. _N→U reaches the zero value at the mid-denaturant concentration (C_m) where 50% of the population is folded and the other 50% is unfolded.