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- W3023782854 abstract "Chemical and thermal denaturation has been widely used in order to investigate the folding processes of proteins in vitro. However, a comprehensive understanding of relationship between chemical and thermal perturbations of proteins at molecular level has been challenging. Here, we have used combined computational and experimental approaches to investigate the denaturing effect on structurally different, unrelated proteins. We have identified a linear relationship between thermal denaturation and chemical denaturation through the stability of protein folding (ΔG) by relating the dependence of ΔG on temperature in the Gibbs-Helmholtz equation and that of ΔG on urea concentration in the linear extrapolation method. We have tested this relationship on apoazurin, cytochrome c and apoflavodoxin by examining their structural similarities of the ensembles perturbed by chemical versus thermal means using coarse-grained molecular simulations at a broad range of urea concentration and temperature. We have found that the temperature of a system in the absence of urea at Tb is linearly proportional to the temperature of the same system under low urea concentration at Tu at a slope of one. The slope of this linear correspondence deviates from one at high urea concentration. In addition, the folding route of apoflavodoxin that involves topological frustration is influenced by the presence of urea. This in silico finding has agreed with in vitro far UV circular dichorism data for apoazurin and cytochrome c. Thus, chemical and thermal unfolding processes correlate in terms of thermodynamics and structural ensembles at most conditions, but deviations occur at high concentrations of denaturant." @default.
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- W3023782854 date "2012-01-01" @default.
- W3023782854 modified "2023-09-29" @default.
- W3023782854 title "Comparison of Chemical and Thermal Protein Denaturation by Combination of Computational and Experimental Approaches" @default.
- W3023782854 doi "https://doi.org/10.1016/j.bpj.2011.11.2510" @default.
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