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Incorporation of Outer Membrane Protein OmpG in Lipid Membranes : Protein-lipid Interactions and β-Barrel Orientation

Incorporation of Outer Membrane Protein OmpG in Lipid Membranes : Protein-lipid Interactions and β-Barrel Orientation

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ANBAZHAGAN, Veerappan, J. QU, Jörg H. KLEINSCHMIDT, Derek MARSH, 2008. Incorporation of Outer Membrane Protein OmpG in Lipid Membranes : Protein-lipid Interactions and β-Barrel Orientation. In: Biochemistry. 47(23), pp. 6189-6198. ISSN 0006-2960. eISSN 1520-4995

@article{Anbazhagan2008Incor-7329, title={Incorporation of Outer Membrane Protein OmpG in Lipid Membranes : Protein-lipid Interactions and β-Barrel Orientation}, year={2008}, number={23}, volume={47}, issn={0006-2960}, journal={Biochemistry}, pages={6189--6198}, author={Anbazhagan, Veerappan and Qu, J. and Kleinschmidt, Jörg H. and Marsh, Derek} }

<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/123456789/7329"> <dc:creator>Qu, J.</dc:creator> <dcterms:bibliographicCitation>First publ. in: Biochemistry ; 47 (2008), 23. - S. 6189 6198</dcterms:bibliographicCitation> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7329/1/bi800203g_OmpG_printed_paper.pdf"/> <dc:contributor>Marsh, Derek</dc:contributor> <dc:format>application/pdf</dc:format> <dcterms:title>Incorporation of Outer Membrane Protein OmpG in Lipid Membranes : Protein-lipid Interactions and β-Barrel Orientation</dcterms:title> <dc:language>eng</dc:language> <dc:creator>Marsh, Derek</dc:creator> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7329"/> <dc:contributor>Qu, J.</dc:contributor> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103416863-3868037-7"/> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Kleinschmidt, Jörg H.</dc:contributor> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7329/1/bi800203g_OmpG_printed_paper.pdf"/> <dc:creator>Kleinschmidt, Jörg H.</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:35Z</dc:date> <dc:creator>Anbazhagan, Veerappan</dc:creator> <dcterms:abstract xml:lang="eng">OmpG is an intermediate size, monomeric, outer membrane protein from Escherichia coli, with nβ ) 14 β-strands. It has a large pore that is amenable to modification by protein engineering. The stoichiometry (Nb ) 20) and selectivity (Kr ) 0.7-1.2) of lipid-protein interaction with OmpG incorporated in dimyristoyl phosphatidylcholine bilayer membranes was determined with various 14-position spinlabeled lipids by using EPR spectroscopy. The limited selectivity for different lipid species is consistent with the disposition of charged residues in the protein. The conformation and orientation (β-strand tilt and β-barrel order parameters) of OmpG in disaturated phosphatidylcholines of odd and even chain lengths from C(12:0) to C(17:0) was determined from polarized infrared spectroscopy of the amide I and amide II bands. A discontinuity in the protein orientation (deduced from the β-barrel order parameters) is observed at the point of hydrophobic matching of the protein with lipid chain length. Compared with smaller (OmpA; nβ ) 8) and larger (FhuA; nβ ) 22) monomeric E. coli outer membrane proteins, the stoichiometry of motionally restricted lipids increases linearly with the number of β-strands, the tilt (β ∼ 44°) of the β-strands is comparable for the three proteins, and the order parameter of the β-barrel increases regularly with nβ. These systematic features of the integration of monomeric β-barrel proteins in lipid membranes could be useful for characterizing outer membrane proteins of unknown structure.</dcterms:abstract> <dc:contributor>Anbazhagan, Veerappan</dc:contributor> <dcterms:issued>2008</dcterms:issued> </rdf:Description> </rdf:RDF>

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