ArticleScientific reports2016
Biological insertion of computationally designed short transmembrane segments.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Living at the border: biophysical gateways into membrane protein insertion and folding.Biophysical reviews · 2026Review
- Structural and functional insights from the sequences and complex domain architecture of adhesin-like proteins fromFrontiers in microbiology · 2024Article
- Folding and Insertion of Transmembrane Helices at the ER.International journal of molecular sciences · 2021Review
- Article
- Transmembrane but not soluble helices fold inside the ribosome tunnel.Nature communications · 2018Article
- The importance of the membrane interface as the reference state for membrane protein stability.Biochimica et biophysica acta. Biomembranes · 2018Article
- The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexity.Scientific reports · 2018Article
- Article
- NMR Investigation of Structures of G-protein Coupled Receptor Folding Intermediates.The Journal of biological chemistry · 2016Article
- The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The great majority of helical membrane proteins are inserted co-translationally into the ER membrane through a continuous ribosome-translocon channel. The efficiency of membrane insertion depends on transmembrane (TM) helix amino acid composition, the helix length and the position of the amino acids within the helix. In this work, we conducted a computational analysis of the composition and location of amino acids in transmembrane helices found in membrane proteins of known structure to obtain an extensive set of designed polypeptide segments with naturally occurring amino acid distributions. Then, using an in vitro translation system in the presence of biological membranes, we experimentally validated our predictions by analyzing its membrane integration capacity. Coupled with known strategies to control membrane protein topology, these findings may pave the way to de novo membrane protein design.
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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.