ArticleNature chemical biology2016
Steric trapping reveals a cooperativity network in the intramembrane protease GlpG.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Article
- Scalable production of monovalent streptavidin with high yield and purity.Scientific reports · 2026Article
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Packing of apolar amino acids is not a strong stabilizing force in transmembrane helix dimerization.Biophysical journal · 2025Article
- The lipid bilayer strengthens the cooperative network of membrane proteins.Science advances · 2025Article
- Oxidative photocatalysis on membranes triggers non-canonical pyroptosis.Nature communications · 2024Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024Review
- Topological deep learning based deep mutational scanning.Computers in biology and medicine · 2023Article
- Interpreting the molecular mechanisms of disease variants in human transmembrane proteins.Biophysical journal · 2023Article
- Thermodynamic analysis of the GASBiophysical journal · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- 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
- Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Spiers Memorial Lecture: Analysis andFaraday discussions · 2021Article
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8 authors.
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Abstract
Membrane proteins are assembled through balanced interactions among proteins, lipids and water. Studying their folding while maintaining the native lipid environment is necessary but challenging. Here we present methods for analyzing key elements of membrane protein folding including thermodynamic stability, compactness of the unfolded state and folding cooperativity under native conditions. The methods are based on steric trapping, which couples the unfolding of a doubly biotinylated protein to the binding of monovalent streptavidin (mSA). We further advanced this technology for general application by developing versatile biotin probes possessing spectroscopic reporters that are sensitized by mSA binding or protein unfolding. By applying these methods to the Escherichia coli intramembrane protease GlpG, we elucidated a widely unraveled unfolded state, subglobal unfolding of the region encompassing the active site, and a network of cooperative and localized interactions to maintain stability. These findings provide crucial insights into the folding energy landscape of membrane proteins.
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