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Membrane proteins: from bench to bits
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2011 (English)In: Biochemical Society Transactions, ISSN 0300-5127, E-ISSN 1470-8752, Vol. 39, 747-750 p.Article in journal (Refereed) Published
Abstract [en]

Membrane proteins currently receive a lot of attention, in large part thanks to a steady stream of high-resolution X-ray structures. Although the first few structures showed proteins composed of tightly packed bundles of very hydrophobic more or less straight transmembrane alpha-helices, we now know that helix-bundle membrane proteins can be both highly flexible and contain transmembrane segments that are neither very hydrophobic nor necessarily helical throughout their lengths. This raises questions regarding how membrane proteins are inserted into the membrane and fold in vivo, and also complicates life for bioinformaticians trying to predict membrane protein topology and structure.

Place, publisher, year, edition, pages
2011. Vol. 39, 747-750 p.
Keyword [en]
hydrophobicity, membrane insertion, membrane protein, protein folding, topology
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-67841DOI: 10.1042/BST0390747ISI: 000292238100007OAI: oai:DiVA.org:su-67841DiVA: diva2:471707
Funder
EU, European Research Council, 232648
Note

authorCount :1

Available from: 2012-01-02 Created: 2012-01-02 Last updated: 2017-12-08Bibliographically approved

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