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Biological insertion of computationally designed short transmembrane segments
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Number of Authors: 4
2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, 23397Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2016. Vol. 6, 23397
National Category
Other Natural Sciences
Identifiers
URN: urn:nbn:se:su:diva-129200DOI: 10.1038/srep23397ISI: 000372483000001PubMedID: 26987712OAI: oai:DiVA.org:su-129200DiVA: diva2:934746
Available from: 2016-06-09 Created: 2016-04-17 Last updated: 2016-06-09Bibliographically approved

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