ArticleNature chemical biology2015
Mapping the energy landscape for second-stage folding of a single membrane protein.
Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 90 citations in OpenAlex.
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Protein force spectroscopy using magnetic tweezers: Slow and steady wins the race?Biophysical journal · 2026Review
- 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
- A UBH-UBX module amplifies p97/VCP's unfolding power to facilitate protein extraction and degradation.Nature communications · 2025Article
- Single-molecule tweezers decode hidden dimerization patterns of membrane proteins within lipid bilayers.Nature communications · 2025Article
- The lipid bilayer strengthens the cooperative network of membrane proteins.Science advances · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- Advancing membrane biology: single-molecule approaches meet model membrane systems.BMB reports · 2025Review
- Probing the energy barriers and stages of membrane protein unfolding using solid-state NMR spectroscopy.Science advances · 2024Article
- 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
- Interpreting the molecular mechanisms of disease variants in human transmembrane proteins.Biophysical journal · 2023Article
- Robust membrane protein tweezers reveal the folding speed limit of helical membrane proteins.eLife · 2023Article
- 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
- Thermodynamic architecture and conformational plasticity of GPCRs.Nature communications · 2023Article
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- Stepwise membrane binding of extended synaptotagmins revealed by optical tweezers.Nature chemical biology · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Membrane proteins are designed to fold and function in a lipid membrane, yet folding experiments within a native membrane environment are challenging to design. Here we show that single-molecule forced unfolding experiments can be adapted to study helical membrane protein folding under native-like bicelle conditions. Applying force using magnetic tweezers, we find that a transmembrane helix protein, Escherichia coli rhomboid protease GlpG, unfolds in a highly cooperative manner, largely unraveling as one physical unit in response to mechanical tension above 25 pN. Considerable hysteresis is observed, with refolding occurring only at forces below 5 pN. Characterizing the energy landscape reveals only modest thermodynamic stability (ΔG = 6.5 kBT) but a large unfolding barrier (21.3 kBT) that can maintain the protein in a folded state for long periods of time (t1/2 ∼3.5 h). The observed energy landscape may have evolved to limit the existence of troublesome partially unfolded states and impart rigidity to the structure.
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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.