Orientation of beta-Barrel Proteins OmpA and FhuA in Lipid Membranes : Chain Length Dependence from Infrared Dichroism

Ramakrishnan, Muthu; Qu, Jian; Pocanschi, Cosmin L.; Kleinschmidt, Jörg; Marsh, Derek

Orientation of beta-Barrel Proteins OmpA and FhuA in Lipid Membranes : Chain Length Dependence from Infrared Dichroism

Dateien

Orientation_of_beta_Barrel_Proteins_OmpA_and_FhuA_in_Lipid_Membranes.pdf(156.19 KB)

Datum

2005

Autor:innen

Ramakrishnan, Muthu

Qu, Jian

Pocanschi, Cosmin L.

Kleinschmidt, Jörg

Marsh, Derek

Publikationstyp

Zeitschriftenartikel

Erschienen in

Biochemistry ; 44 (2005), 9. - S. 3515-3523. - ISSN 0006-2960. - eISSN 1520-4995

Zusammenfassung

The outer-membrane proteins OmpA and FhuA of Escherichia coli are monomeric β-barrels of widely differing size. Polarized attenuated totalreflection infrared spectroscopy has been used to determine the orientation of the β-barrels in phosphatidylcholine host matrices of different lipid chain lengths. The linear dichroism of the amide I band from OmpA and FhuA in hydrated membranes generally increases with increasing chain length from diC(12:0) to diC(17:0) phosphatidylcholine, in both the fluid and gel phases. Measurements of the amide I and amide II dichroism from dry samples are used to deduce the strand tilt (β) 46° for OmpA and β = 44.5° for FhuA). These values are then used to deduce the order parameters, P2(cos α) , of the β-barrels from the amide I dichroic ratios of the hydrated membranes. The orientational ordering of the β-barrels and their assembly in the membrane are discussed in terms of hydrophobic matching with the lipid chains.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

RAMAKRISHNAN, Muthu, Jian QU, Cosmin L. POCANSCHI, Jörg KLEINSCHMIDT, Derek MARSH, 2005. Orientation of beta-Barrel Proteins OmpA and FhuA in Lipid Membranes : Chain Length Dependence from Infrared Dichroism. In: Biochemistry. 44(9), pp. 3515-3523. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi047603y

BibTex

@article{Ramakrishnan2005Orien-8130,
  year={2005},
  doi={10.1021/bi047603y},
  title={Orientation of beta-Barrel Proteins OmpA and FhuA in Lipid Membranes : Chain Length Dependence from Infrared Dichroism},
  number={9},
  volume={44},
  issn={0006-2960},
  journal={Biochemistry},
  pages={3515--3523},
  author={Ramakrishnan, Muthu and Qu, Jian and Pocanschi, Cosmin L. and Kleinschmidt, Jörg and Marsh, Derek}
}

RDF

<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/server/rdf/resource/123456789/8130">
    <dc:creator>Kleinschmidt, Jörg</dc:creator>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:contributor>Pocanschi, Cosmin L.</dc:contributor>
    <dcterms:title>Orientation of beta-Barrel Proteins OmpA and FhuA in Lipid Membranes : Chain Length Dependence from Infrared Dichroism</dcterms:title>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8130/1/Orientation_of_beta_Barrel_Proteins_OmpA_and_FhuA_in_Lipid_Membranes.pdf"/>
    <dc:contributor>Qu, Jian</dc:contributor>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:language>eng</dc:language>
    <dcterms:bibliographicCitation>First publ. in: Biochemistry ; 44 (2005), 9. - S. 3515-3523</dcterms:bibliographicCitation>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8130/1/Orientation_of_beta_Barrel_Proteins_OmpA_and_FhuA_in_Lipid_Membranes.pdf"/>
    <dc:format>application/pdf</dc:format>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8130"/>
    <dcterms:issued>2005</dcterms:issued>
    <dc:contributor>Kleinschmidt, Jörg</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:40:50Z</dc:date>
    <dc:contributor>Ramakrishnan, Muthu</dc:contributor>
    <dc:contributor>Marsh, Derek</dc:contributor>
    <dc:creator>Qu, Jian</dc:creator>
    <dcterms:abstract xml:lang="eng">The outer-membrane proteins OmpA and FhuA of Escherichia coli are monomeric β-barrels of widely differing size. Polarized attenuated totalreflection infrared spectroscopy has been used to determine the orientation of the β-barrels in phosphatidylcholine host matrices of different lipid chain lengths. The linear dichroism of the amide I band from OmpA and FhuA in hydrated membranes generally increases with increasing chain length from diC(12:0) to diC(17:0) phosphatidylcholine, in both the fluid and gel phases. Measurements of the amide I and amide II dichroism from dry samples are used to deduce the strand tilt (β) 46° for OmpA and β = 44.5° for FhuA). These values are then used to deduce the order parameters,  P2(cos α) , of the β-barrels from the amide I dichroic ratios of the hydrated membranes. The orientational ordering of the β-barrels and their assembly in the membrane are discussed in terms of hydrophobic matching with the lipid chains.</dcterms:abstract>
    <dc:creator>Ramakrishnan, Muthu</dc:creator>
    <dc:creator>Marsh, Derek</dc:creator>
    <dc:creator>Pocanschi, Cosmin L.</dc:creator>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Ja