ArticleProceedings of the National Academy of Sciences of the United States of America2013
Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 116 citations in OpenAlex.
- Linking multipoint folding and stability with functional regulation in the mitochondrial transmembrane β-barrel Sam50.Nature communications · 2026Article
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Membrane insertion and dimerization of glycophorin-A mutations studied by free energy simulations.Biophysical journal · 2026Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Sculpting conducting nanopore size and shape through de novo protein design.Science (New York, N.Y.) · 2024Article
- Sculpting conducting nanopore size and shape throughbioRxiv : the preprint server for biology · 2023Article
- The Thermodynamic Stability of Membrane Proteins in Micelles and Lipid Bilayers Investigated with the Ferrichrom Receptor FhuA.The Journal of membrane biology · 2022Article
- Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The sacrificial adaptor protein Skp functions to remove stalled substrates from the β-barrel assembly machine.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Membrane proteins enter the fold.Current opinion in structural biology · 2021Review
- The assembly of β-barrel membrane proteins by BAM and SAM.Molecular microbiology · 2021Review
- De novo design of transmembrane β barrels.Science (New York, N.Y.) · 2021Article
- Evolutionary selection of a 19-stranded mitochondrial β-barrel scaffold bears structural and functional significance.The Journal of biological chemistry · 2020Article
- Structure and Function of the T4 Spackle Protein Gp61.3.Viruses · 2020Article
- Affinity of Skp to OmpC revealed by single-molecule detection.Scientific reports · 2020Article
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy.Angewandte Chemie (International ed. in English) · 2020Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- GeTFEP: A general transfer free energy profile of transmembrane proteins.Protein science : a publication of the Protein Society · 2020Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Thermodynamic stabilities are pivotal for understanding structure-function relationships of proteins, and yet such determinations are rare for membrane proteins. Moreover, the few measurements that are available have been conducted under very different experimental conditions, which compromises a straightforward extraction of physical principles underlying stability differences. Here, we have overcome this obstacle and provided structure-stability comparisons for multiple membrane proteins. This was enabled by measurements of the free energies of folding and the m values for the transmembrane proteins PhoP/PhoQ-activated gene product (PagP) and outer membrane protein W (OmpW) from Escherichia coli. Our data were collected in the same lipid bilayer and buffer system we previously used to determine those parameters for E. coli outer membrane phospholipase A (OmpLA). Biophysically, our results suggest that the stabilities of these proteins are strongly correlated to the water-to-bilayer transfer free energy of the lipid-facing residues in their transmembrane regions. We further discovered that the sensitivities of these membrane proteins to chemical denaturation, as judged by their m values, was consistent with that previously observed for water-soluble proteins having comparable differences in solvent exposure between their folded and unfolded states. From a biological perspective, our findings suggest that the folding free energies for these membrane proteins may be the thermodynamic sink that establishes an energy gradient across the periplasm, thus driving their sorting by chaperones to the outer membranes in living bacteria. Binding free energies of these outer membrane proteins with periplasmic chaperones support this energy sink hypothesis.
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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.