ArticleProtein science : a publication of the Protein Society2012
Revisiting the folding kinetics of bacteriorhodopsin.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 39 citations in OpenAlex.
- Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024Review
- Cys-labeling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes?Biophysical journal · 2021Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Bicelle size modulates the rate of bacteriorhodopsin folding.Protein science : a publication of the Protein Society · 2018Article
- Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Scientific reports · 2015Article
- Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The observation of evolutionary interaction pattern pairs in membrane proteins.BMC structural biology · 2015Article
- The safety dance: biophysics of membrane protein folding and misfolding in a cellular context.Quarterly reviews of biophysics · 2015Article
- Bacteriorhodopsin folds through a poorly organized transition state.Journal of the American Chemical Society · 2014Article
- Renaturing membrane proteins in the lipid cubic phase, a nanoporous membrane mimetic.Scientific reports · 2014Article
- Measuring membrane protein stability under native conditions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Influence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2.PloS one · 2014Article
- Thermostabilization of the β1-adrenergic receptor correlates with increased entropy of the inactive state.The journal of physical chemistry. B · 2013Article
- Reversible folding of human peripheral myelin protein 22, a tetraspan membrane protein.Biochemistry · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
The elucidation of the physical principles that govern the folding and stability of membrane proteins is one of the greatest challenges in protein science. Several insights into the folding of α-helical membrane proteins have come from the investigation of the conformational equilibrium of H. halobium bacteriorhodopsin (bR) in mixed micelles using SDS as a denaturant. In an effort to confirm that folded bR and SDS-denatured bR reach the same conformational equilibrium, we found that bR folding is significantly slower than has been previously known. Interrogation of the effect of the experimental variables on folding kinetics reveals that the rate of folding is dependent not only on the mole fraction of SDS but also on the molar concentrations of mixed micelle components, a variable that was not controlled in the previous study of bR folding kinetics. Moreover, when the molar concentrations of mixed micelle components are fixed at the concentrations commonly employed for bR equilibrium studies, conformational relaxation in the transition zone is slower than hydrolysis of the retinal Schiff base. As a result, the conformational equilibrium between folded bR and SDS-denatured bR cannot be achieved under the conventional condition. Our finding suggests that the molar concentrations of mixed micelle components are important experimental variables in the investigation of the kinetics and thermodynamics of bR folding and should be accounted for to ensure the accurate assessment of the conformational equilibrium of bR without the interference of retinal hydrolysis.
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