ArticleNature communications2019
Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Probing the energy barriers and stages of membrane protein unfolding using solid-state NMR spectroscopy.Science advances · 2024Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Measurement of Residual Dipolar Couplings Using Magnetically Aligned and Flipped Nanodiscs.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Biological solid-state NMR: Integrative across different scientific disciplines.Journal of structural biology: X · 2022Article
- Identification of Thermal Conduits That Link the Protein-Water Interface to the Active Site Loop and Catalytic Base in Enolase.Journal of the American Chemical Society · 2021Article
- Dynamic Nuclear Polarization of Biomembrane Assemblies.Biomolecules · 2020Article
- Recent Advances in Chemical Biology Using Benzophenones and Diazirines as Radical Precursors.Molecules (Basel, Switzerland) · 2020Review
- Templated folding of intrinsically disordered proteins.The Journal of biological chemistry · 2020Review
- Magnetic Alignment of Polymer Nanodiscs Probed by Solid-State NMR Spectroscopy.Langmuir : the ACS journal of surfaces and colloids · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane protein folding, structure, and function strongly depend on a cell membrane environment, yet detailed characterization of folding within a lipid bilayer is challenging. Studies of reversible unfolding yield valuable information on the energetics of folding and on the hierarchy of interactions contributing to protein stability. Here, we devise a methodology that combines hydrogen-deuterium (H/D) exchange and solid-state NMR (SSNMR) to follow membrane protein unfolding in lipid membranes at atomic resolution through detecting changes in the protein water-accessible surface, and concurrently monitoring the reversibility of unfolding. We obtain atomistic description of the reversible part of a thermally induced unfolding pathway of a seven-helical photoreceptor. The pathway is visualized through SSNMR-detected snapshots of H/D exchange patterns as a function of temperature, revealing the unfolding intermediate and its stabilizing factors. Our approach is transferable to other membrane proteins, and opens additional ways to characterize their unfolding and stabilizing interactions with atomic resolution.
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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.