ArticleProceedings of the National Academy of Sciences of the United States of America2010
On the energetics of translocon-assisted insertion of charged transmembrane helices into membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 45 citations in OpenAlex.
- Living at the border: biophysical gateways into membrane protein insertion and folding.Biophysical reviews · 2026Review
- 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
- The importance of the membrane interface as the reference state for membrane protein stability.Biochimica et biophysica acta. Biomembranes · 2018Article
- Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane.Biophysical journal · 2018Article
- Transmembrane helices containing a charged arginine are thermodynamically stable.European biophysics journal : EBJ · 2017Article
- Structurally detailed coarse-grained model for Sec-facilitated co-translational protein translocation and membrane integration.PLoS computational biology · 2017Article
- Simulating the Function of the MjNhaP1 Transporter.The journal of physical chemistry. B · 2016Article
- Article
- Simulating the function of sodium/proton antiporters.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Anomalous behavior of water inside the SecY translocon.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Multiscale modeling of biological functions: from enzymes to molecular machines (Nobel Lecture).Angewandte Chemie (International ed. in English) · 2014Article
- Spontaneous transmembrane helix insertion thermodynamically mimics translocon-guided insertion.Nature communications · 2014Article
- Folding of Aquaporin 1: multiple evidence that helix 3 can shift out of the membrane core.Protein science : a publication of the Protein Society · 2014Article
- An effective coarse-grained model for biological simulations: recent refinements and validations.Proteins · 2014Article
- On the nature of the apparent free energy of inserting amino acids into membrane through the translocon.The journal of physical chemistry. B · 2013Article
- Effects of flanking loops on membrane insertion of transmembrane helices: a role for peptide conformational equilibrium.The journal of physical chemistry. B · 2013Article
- Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations.International journal of molecular sciences · 2013Article
- Simulating the pulling of stalled elongated peptide from the ribosome by the translocon.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Reconciling the roles of kinetic and thermodynamic factors in membrane-protein insertion.Journal of the American Chemical Society · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The understanding of the mechanism of insertion of transmembrane (TM) helixes through the translocon presents a major open challenge. Although the experimental information about the partition of the inserted helices between the membrane and the solution contains crucial information about this process, it is not clear how to extract this information. In particular, it is not clear how to rationalize the small apparent insertion energy, ΔG(app), of an ionized residue in the center of a TM helix. Here we explore the nature of the insertion energies, asking what should be the value of these parameters if their measurements represent equilibrium conditions. This is done using a coarse-grained model with advanced electrostatic treatment. Estimating the energetics of ionized arginine of a TM helix in the presence of neighboring helixes or the translocon provides a rationale for the observed ΔG(app) of ionized residues. It is concluded that the apparent insertion free energy of TM with charged residues reflects probably more than just the free energy of moving the isolate single helix from water into the membrane. The present approach should be effective not only in exploring the mechanism of the operation of the translocon but also for studies of other membrane proteins.
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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.