ArticleJournal of the American Chemical Society2014
Bacteriorhodopsin folds through a poorly organized transition state.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Quantifying a light-induced energetic change in bacteriorhodopsin by force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation.International journal of molecular sciences · 2023Article
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Untangling the complexity of membrane protein folding.Current opinion in structural biology · 2022Review
- 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
- The high-energy transition state of the glutamate transporter homologue GltPh.The EMBO journal · 2021Article
- A complete picture of protein unfolding and refolding in surfactants.Chemical science · 2019Article
- Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway.Nature communications · 2019Article
- Molecular mechanism for thermal denaturation of thermophilic rhodopsin.Chemical science · 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
- Kinetic stability of membrane proteins.Biophysical reviews · 2017Review
- Documentation of an Imperative To Improve Methods for Predicting Membrane Protein Stability.Biochemistry · 2016Article
- Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Kinetics of peptide folding in lipid membranes.Biopolymers · 2015Review
- 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
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The folding mechanisms of helical membrane proteins remain largely uncharted. Here we characterize the kinetics of bacteriorhodopsin folding and employ φ-value analysis to explore the folding transition state. First, we developed and confirmed a kinetic model that allowed us to assess the rate of folding from SDS-denatured bacteriorhodopsin (bRU) and provides accurate thermodynamic information even under influence of retinal hydrolysis. Next, we obtained reliable φ-values for 16 mutants of bacteriorhodopsin with good coverage across the protein. Every φ-value was less than 0.4, indicating the transition state is not uniquely structured. We suggest that the transition state is a loosely organized ensemble of conformations.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.