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A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and crystallization

A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and crystallization

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HOVERS, Jens, Meike POTSCHIES, Ange POLIDORI, Bernard PUCCI, Simon RAYNAL, Francoise BONNETÉ, Maria J. SERRANO-VEGA, Christopher G. TATE, Daniel PICOT, Jean-Luc POPOT, Rony NEHMÉ, Michel BIDET, Isabelle MUS-VETEAU, Holger BUSSKAMP, Karl-Heinz JUNG, Andreas MARX, Peter A. TIMMINS, Wolfram WELTE, 2011. A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and crystallization. In: Molecular Membrane Biology. 28(3), pp. 171-181. ISSN 0968-7688. eISSN 1464-5203. Available under: doi: 10.3109/09687688.2011.552440

@article{Hovers2011-04class-13988, title={A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and crystallization}, year={2011}, doi={10.3109/09687688.2011.552440}, number={3}, volume={28}, issn={0968-7688}, journal={Molecular Membrane Biology}, pages={171--181}, author={Hovers, Jens and Potschies, Meike and Polidori, Ange and Pucci, Bernard and Raynal, Simon and Bonneté, Francoise and Serrano-Vega, Maria J. and Tate, Christopher G. and Picot, Daniel and Popot, Jean-Luc and Nehmé, Rony and Bidet, Michel and Mus-Veteau, Isabelle and Bußkamp, Holger and Jung, Karl-Heinz and Marx, Andreas and Timmins, Peter A. and Welte, Wolfram} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/13988"> <dcterms:title>A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and crystallization</dcterms:title> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-07-21T09:24:39Z</dcterms:available> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:creator>Raynal, Simon</dc:creator> <dc:creator>Serrano-Vega, Maria J.</dc:creator> <dc:contributor>Raynal, Simon</dc:contributor> <dc:contributor>Polidori, Ange</dc:contributor> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Bonneté, Francoise</dc:creator> <dc:creator>Tate, Christopher G.</dc:creator> <dcterms:bibliographicCitation>Publ. in: Molecular Membrane Biology 28 (2011), 3, pp. 171-181</dcterms:bibliographicCitation> <dc:creator>Bidet, Michel</dc:creator> <dc:contributor>Popot, Jean-Luc</dc:contributor> <dc:creator>Marx, Andreas</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/13988"/> <dc:creator>Welte, Wolfram</dc:creator> <dc:creator>Timmins, Peter A.</dc:creator> <dc:creator>Bußkamp, Holger</dc:creator> <dcterms:abstract xml:lang="eng">Mixed protein-surfactant micelles are used for in vitro studies and 3D crystallization when solutions of pure, monodisperse integral membrane proteins are required. However, many membrane proteins undergo inactivation when transferred from the biomembrane into micelles of conventional surfactants with alkyl chains as hydrophobic moieties. Here we describe the development of surfactants with rigid, saturated or aromatic hydrocarbon groups as hydrophobic parts. Their stabilizing properties are demonstrated with three different integral membrane proteins. The temperature at which 50% of the binding sites for specific ligands are lost is used as a measure of stability and dodecyl-β-D-maltoside (‘C12-b-M’) as a reference for conventional surfactants. One surfactant increased the stability of two different G protein-coupled receptors and the human Patched protein receptor by approximately 10°C compared to C12-b-M. Another surfactant yielded the highest stabilization of the human Patched protein receptor compared to C12-b-M (13°C) but was inferior for the G protein-coupled receptors. In addition, one of the surfactants was successfully used to stabilize and crystallize the cytochrome b6 f complex from Chlamydomonas reinhardtii. The structure was solved to the same resolution as previously reported in C12-b-M.</dcterms:abstract> <dc:contributor>Nehmé, Rony</dc:contributor> <dc:contributor>Welte, Wolfram</dc:contributor> <dc:contributor>Timmins, Peter A.</dc:contributor> <dc:creator>Picot, Daniel</dc:creator> <dc:contributor>Bußkamp, Holger</dc:contributor> <dc:creator>Nehmé, Rony</dc:creator> <dc:contributor>Mus-Veteau, Isabelle</dc:contributor> <dc:contributor>Bonneté, Francoise</dc:contributor> <dc:language>eng</dc:language> <dc:contributor>Bidet, Michel</dc:contributor> <dc:creator>Popot, Jean-Luc</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-07-21T09:24:39Z</dc:date> <dc:contributor>Hovers, Jens</dc:contributor> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:contributor>Marx, Andreas</dc:contributor> <dc:creator>Hovers, Jens</dc:creator> <dc:creator>Potschies, Meike</dc:creator> <dc:creator>Jung, Karl-Heinz</dc:creator> <dc:contributor>Tate, Christopher G.</dc:contributor> <dc:contributor>Serrano-Vega, Maria J.</dc:contributor> <dc:creator>Polidori, Ange</dc:creator> <dcterms:issued>2011-04</dcterms:issued> <dc:contributor>Pucci, Bernard</dc:contributor> <dc:contributor>Jung, Karl-Heinz</dc:contributor> <dc:creator>Mus-Veteau, Isabelle</dc:creator> <dc:contributor>Picot, Daniel</dc:contributor> <dc:contributor>Potschies, Meike</dc:contributor> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:creator>Pucci, Bernard</dc:creator> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> </rdf:Description> </rdf:RDF>

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