ReviewProtein science : a publication of the Protein Society2015
Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.
Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
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- Packing of apolar amino acids is not a strong stabilizing force in transmembrane helix dimerization.Biophysical journal · 2025Article
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- A Novel Rare PSEN2 Val226Ala in PSEN2 in a Korean Patient with Atypical Alzheimer's Disease, and the Importance of PSEN2 5th Transmembrane Domain (TM5) in AD Pathogenesis.International journal of molecular sciences · 2024Article
- Structural and functional insights from the sequences and complex domain architecture of adhesin-like proteins fromFrontiers in microbiology · 2024Article
- Case report: Double mutations in a patient with early-onset Alzheimer's disease in China, PSEN2 and IDE variants.Frontiers in neuroscience · 2024Article
- The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins.Membranes · 2022Article
- Kassporin-KS1: A Novel Pentadecapeptide from the Skin Secretion ofAntibiotics (Basel, Switzerland) · 2022Article
- Molecular docking and simulation of IcaC protein as O-succinyltransferase function inCurrent research in structural biology · 2022Article
- Discovery and Characterization of the Phospholemman/SIMP/Viroporin Superfamily.Microbial physiology · 2022Article
- Unravelling the molecular effect of ocellatin-1, F1, K1 and S1, the frog-skin antimicrobial peptides to enhance its therapeutics-quantum and molecular mechanical approaches.Journal of molecular modeling · 2021Article
- Membrane Protein Engineering with Rosetta.Methods in molecular biology (Clifton, N.J.) · 2021Article
- The Landscape ofCells · 2020Article
- EtMIC3 and its receptors BAG1 and ENDOUL are essential for site-specific invasion of Eimeria tenella in chickens.Veterinary research · 2020Article
- A comprehensive computational study of amino acid interactions in membrane proteins.Scientific reports · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Interaction mapping of the Sec61 translocon identifies two Sec61α regions interacting with hydrophobic segments in translocating chains.The Journal of biological chemistry · 2018Article
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Authors and funding
2 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Cells have developed an incredible machinery to facilitate the insertion of membrane proteins into the membrane. While we have a fairly good understanding of the mechanism and determinants of membrane integration, more data is needed to understand the insertion of membrane proteins with more complex insertion and folding pathways. This review will focus on marginally hydrophobic transmembrane helices and their influence on membrane protein folding. These weakly hydrophobic transmembrane segments are by themselves not recognized by the translocon and therefore rely on local sequence context for membrane integration. How can such segments reside within the membrane? We will discuss this in the light of features found in the protein itself as well as the environment it resides in. Several characteristics in proteins have been described to influence the insertion of marginally hydrophobic helices. Additionally, the influence of biological membranes is significant. To begin with, the actual cost for having polar groups within the membrane may not be as high as expected; the presence of proteins in the membrane as well as characteristics of some amino acids may enable a transmembrane helix to harbor a charged residue. The lipid environment has also been shown to directly influence the topology as well as membrane boundaries of transmembrane helices-implying a dynamic relationship between membrane proteins and their environment.
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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.