ArticleBiochimica et biophysica acta2012
Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state.
Article in Biochimica et biophysica acta, 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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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Free-energy changes of bacteriorhodopsin point mutants measured by single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway.Nature communications · 2019Article
- 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
- Documentation of an Imperative To Improve Methods for Predicting Membrane Protein Stability.Biochemistry · 2016Article
- Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III.Biochimica et biophysica acta · 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
- Measuring membrane protein stability under native conditions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- High-resolution optical tweezers for single-molecule manipulation.The Yale journal of biology and medicine · 2013Review
- 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
- Shifting hydrogen bonds may produce flexible transmembrane helices.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Revisiting the folding kinetics of bacteriorhodopsin.Protein science : a publication of the Protein Society · 2012Article
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4 authors at 2 institutions in 1 country.
Funding
Abstract
The stability of bacteriorhodopsin (bR) has often been assessed using SDS unfolding assays that monitor the transition of folded bR (bR(f)) to unfolded (bR(u)). While many criteria suggest that the unfolding curves reflect thermodynamic stability, slow retinal (RET) hydrolysis during refolding makes it impossible to perform the most rigorous test for equilibrium, i.e., superimposable unfolding and refolding curves. Here we made a new equilibrium test by asking whether the refolding rate in the transition zone is faster than RET hydrolysis. We find that under conditions we have used previously, refolding is in fact slower than hydrolysis, strongly suggesting that equilibrium is not achieved. Instead, the apparent free energy values reported previously are dominated by unfolding rates. To assess how different the true equilibrium values are, we employed an alternative method by measuring the transition of bR(f) to unfolded bacterioopsin (bO(u)), the RET-free form of unfolded protein. The bR(f)-to-bO(u) transition is fully reversible, particular when we add excess RET. We compared the difference in unfolding free energies for 13 bR mutants measured by both assays. For 12 of the 13 mutants with a wide range of stabilities, the results are essentially the same within experimental error. The congruence of the results is fortuitous and suggests the energetic effects of most mutations may be focused on the folded state. The bR(f)-to-bO(u) reaction is inconvenient because many days are required to reach equilibrium, but it is the preferable measure of thermodynamic stability. This article is part of a Special Issue entitled: Protein Folding in Membranes.
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