ArticleProceedings of the National Academy of Sciences of the United States of America2011
Free-energy cost for translocon-assisted insertion of membrane proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 69 citations in OpenAlex.
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Functional diversity in GII.4 norovirus entry: HBGA binding and capsid clustering dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Bioenergetics and the Evolution of Cellular Traits.Annual review of biophysics · 2025Review
- Alchemical Free Energy Calculations on Membrane-Associated Proteins.Journal of chemical theory and computation · 2023Review
- PEO-Biomacromolecules · 2022Article
- Three-stage model of helical membrane protein folding: Role of membrane-water interface as the intermediate stage vestibule for TM helices during their in membrano assembly.Biochemical and biophysical research communications · 2022Article
- Accurate Binding Free Energy Method from End-State MD Simulations.Journal of chemical information and modeling · 2022Article
- Vectorial insertion of a β-helical peptide into membrane: a theoretical study on polytheonamide B.Biophysical journal · 2021Article
- Energetics of stochastic BCM type synaptic plasticity and storing of accurate information.Journal of computational neuroscience · 2021Article
- Characterization of the Features of Water Inside the SecY Translocon.The Journal of membrane biology · 2021Review
- Dynamics of Co-translational Membrane Protein Integration and Translocation via the Sec Translocon.Journal of the American Chemical Society · 2020Review
- Quantitative Characterization of Protein-Lipid Interactions by Free Energy Simulation between Binary Bilayers.Journal of chemical theory and computation · 2019Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- The importance of the membrane interface as the reference state for membrane protein stability.Biochimica et biophysica acta. Biomembranes · 2018Article
- Computed Free Energies of Peptide Insertion into Bilayers are Independent of Computational Method.The Journal of membrane biology · 2018Article
- Transmembrane helices containing a charged arginine are thermodynamically stable.European biophysics journal : EBJ · 2017Article
- Evaluation of the hybrid resolution PACE model for the study of folding, insertion, and pore formation of membrane associated peptides.Journal of computational chemistry · 2017Article
- Structurally detailed coarse-grained model for Sec-facilitated co-translational protein translocation and membrane integration.PLoS computational biology · 2017Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Nascent membrane proteins typically insert in a sequential fashion into the membrane via a protein-conducting channel, the Sec translocon. How this process occurs is still unclear, although a thermodynamic partitioning between the channel and the membrane environment has been proposed. Experiment- and simulation-based scales for the insertion free energy of various amino acids are, however, at variance, the former appearing to lie in a narrower range than the latter. Membrane insertion of arginine, for instance, requires 14-17 kcal/mol according to molecular dynamics simulations, but only 2-3 kcal/mol according to experiment. We suggest that this disagreement is resolved by assuming a two-stage insertion process wherein the first step, the insertion into the translocon, is energized by protein synthesis and, therefore, has an effectively zero free-energy cost; the second step, the insertion into the membrane, invokes the translocon as an intermediary between the fully hydrated and the fully inserted locations. Using free-energy perturbation calculations, the effective transfer free energies from the translocon to the membrane have been determined for both arginine and leucine amino acids carried by a background polyleucine helix. Indeed, the insertion penalty for arginine as well as the insertion gain for leucine from the translocon to the membrane is found to be significantly reduced compared to direct insertion from water, resulting in the same compression as observed in the experiment-based scale.
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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.