Journal article
Protein conformational stabilities can be determined from hydrogen exchange rates
Nature structural biology, Vol.6(10), pp.910-912
10/01/1999
DOI: 10.1038/13273
PMID: 10504722
Abstract
Measuring protein conformational stability is one key to solving the protein folding problem. The conformational stability is the free energy change of the unfolding reaction, F ↔ U, under ambient conditions, ΔGU = GU - GF. Traditional methods of measuring ΔGU are solvent (urea or guanidinium chloride (GdmCl)) or thermal denaturation1. Solvent denaturation curves are generally analyzed using the linear extrapolation method (LEM): ΔG = ΔGU(H2O) - m[denaturant] (1) where m is a measure of the dependence of ΔG on denaturant, and ΔGU(H2O) is an estimate of the conformational stability that assumes that the linear dependence of ΔG on denaturant observed in the transition region continues to 0 M denaturant. Thermal denaturation experiments yield the melting temperature, Tm, the enthalpy change at Tm, ΔHm, and the heat capacity change, ΔCp, which can then be used to calculate ΔGU at any temperature T, ΔGU(T), with the Gibbs–Helmholtz equation: ΔGU(T) = ΔHm(1 - T/Tm) + ΔCp[T - Tm - T ln (T/Tm)] (2)
Details
- Title: Subtitle
- Protein conformational stabilities can be determined from hydrogen exchange rates
- Creators
- BMP Huyghues-DespointesJ M Scholtz - Texas A&M UniversityC N Pace
- Resource Type
- Journal article
- Publication Details
- Nature structural biology, Vol.6(10), pp.910-912
- Publisher
- Springer Nature
- DOI
- 10.1038/13273
- PMID
- 10504722
- ISSN
- 1072-8368
- eISSN
- 2331-365X
- Number of pages
- 3
- Language
- English
- Date published
- 10/01/1999
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984288731802771
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