ArticleCommunications biology2020
Free-energy landscapes of membrane co-translocational protein unfolding.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Optical and Electrical Characterization of Nanopores in Freestanding Lipid Bilayers Formed on Microelectrode Cavity Arrays.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Large and Stable Nanopores Formed by Complement Component 9 for Characterizing Single Folded Proteins.ACS nano · 2025Article
- Nanopore DNA sequencing technologies and their applications towards single-molecule proteomics.Nature chemistry · 2024Review
- Unidirectional single-file transport of full-length proteins through a nanopore.Nature biotechnology · 2023Article
- Article
- Herding cats: Label-based approaches in protein translocation through nanopore sensors for single-molecule protein sequence analysis.iScience · 2021Review
- The emerging landscape of single-molecule protein sequencing technologies.Nature methods · 2021Review
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein post-translational translocation is found at the plasma membrane of prokaryotes and protein import into organellae. Translocon structures are becoming available, however the dynamics of proteins during membrane translocation remain largely obscure. Here we study, at the single-molecule level, the folding landscape of a model protein while forced to translocate a transmembrane pore. We use a DNA tag to drive the protein into the α-hemolysin pore under a quantifiable force produced by an applied electric potential. Using a voltage-quench approach we find that the protein fluctuates between the native state and an intermediate in the translocation process at estimated forces as low as 1.9 pN. The fluctuation kinetics provide the free energy landscape as a function of force. We show that our stable, ≈15 k
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