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- W2073629943 abstract "The analytical toolkit developed for investigations into water-soluble protein folding has yet to be applied in earnest to membrane proteins. A major problem is the difficulty in collecting kinetic data, which are crucial to understanding any reaction. Here, we combine kinetic and thermodynamic studies of the reversible unfolding of an α-helical membrane protein to provide a definitive value for the reaction free energy and a means to probe the transition state. Our analyses show that the major unfolding step in the SDS-induced denaturation of bacteriorhodopsin involves a reduction in α-helical structure and proceeds with a large free-energy change; both our equilibrium and kinetic measurements predict that the free energy of unfolding in the absence of denaturant is +20 kcal·mol −1 , with an associated m -value of 25 kcal·mol −1 . The rate of unfolding in the absence of denaturant, k u H 2 O , is surprisingly very slow (≈10 −15 s −1 ). The kinetics also give information on the transition state for this major unfolding step, with a value for β ( m f /[ m f + m u ]) of ≈0.1, indicating that the transition state is close to the unfolded state. We thus present a basis for mapping the structural and energetic properties of membrane protein folding by mutagenesis and classical kinetics." @default.
- W2073629943 created "2016-06-24" @default.
- W2073629943 creator A5067138797 @default.
- W2073629943 creator A5070046456 @default.
- W2073629943 date "2007-11-27" @default.
- W2073629943 modified "2023-10-16" @default.
- W2073629943 title "Combined kinetic and thermodynamic analysis of α-helical membrane protein unfolding" @default.
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- W2073629943 doi "https://doi.org/10.1073/pnas.0705067104" @default.
- W2073629943 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2141892" @default.
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- W2073629943 hasPublicationYear "2007" @default.
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