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Comparison of chemi...
Comparison of chemical and thermal protein denaturation by combination of computational and experimental approaches. II
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Wang, Qian (author)
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Christiansen, Alexander (author)
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Samiotakis, Antonios (author)
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- Wittung-Stafshede, Pernilla (author)
- Umeå universitet,Kemiska institutionen
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Cheung, Margaret S. (author)
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(creator_code:org_t)
- Lancaster, Pa. American Institute of Physics (AIP), 2011
- 2011
- English.
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In: Journal of Chemical Physics. - Lancaster, Pa. : American Institute of Physics (AIP). - 0021-9606 .- 1089-7690. ; 135:17, s. 175102-
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
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- Chemical and thermal denaturation methods have been widely used to investigate folding processes of proteins in vitro. However, a molecular understanding of the relationship between these two perturbation methods is lacking. Here, we combined computational and experimental approaches to investigate denaturing effects on three structurally different proteins. We derived a linear relationship between thermal denaturation at temperature T(b) and chemical denaturation at another temperature T(u) using the stability change of a protein (Delta G). For this, we related the dependence of Delta G on temperature, in the Gibbs-Helmholtz equation, to that of Delta G on urea concentration in the linear extrapolation method, assuming that there is a temperature pair from the urea (T(u)) and the aqueous (T(b)) ensembles that produces the same protein structures. We tested this relationship on apoazurin, cytochrome c, and apoflavodoxin using coarse-grained molecular simulations. We found a linear correlation between the temperature for a particular structural ensemble in the absence of urea, T(b), and the temperature of the same structural ensemble at a specific urea concentration, T(u). The in silico results agreed with in vitro far-UV circular dichroism data on apoazurin and cytochrome c. We conclude that chemical and thermal unfolding processes correlate in terms of thermodynamics and structural ensembles at most conditions; however, deviations were found at high concentrations of denaturant. (C) 2011 American Institute of Physics. [doi: 10.1063/1.3656692]
Subject headings
- NATURVETENSKAP -- Fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences (hsv//eng)
Keyword
- biochemistry
- biological techniques
- biothermics
- circular dichroism
- molecular biophysics
- molecular configurations
- proteins
- reaction kinetics theory
Publication and Content Type
- ref (subject category)
- art (subject category)
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