Abstract
Thermodynamics of protein folding refers to the stability measurements where structural changes of a given protein in the presence of a denaturing agent are monitored by spectroscopic or calorimetric techniques. In macroscopic point of view, protein stability represents the ratio of the population of its unfolded state to that of folded one in equilibrium condition, while in microscopic point of view, the stability is actually a net value from a combination of favorable and unfavorable contributions that affect the structural integrity of a protein molecule. In this manuscript, the principles and methodological aspects of thermodynamic studies and methods of data analysis as well as interpretation of the results are presented.
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b and c were adapted from Pace and Shaw (2000)
Figure was taken from Swint and Robertson (1993)
Figure was adapted from Serdyuk et al. (2007) and presented with some modification
Data were adapted from Griko et al. (1988a) and presented with some modifications
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21 December 2021
A Correction to this paper has been published: https://doi.org/10.1007/s00249-021-01586-6
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Shirdel, S.A., Khalifeh, K. Thermodynamics of protein folding: methodology, data analysis and interpretation of data. Eur Biophys J 48, 305–316 (2019). https://doi.org/10.1007/s00249-019-01362-7
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DOI: https://doi.org/10.1007/s00249-019-01362-7