Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent

Lade...
Vorschaubild
Dateien
Prot.SciS096183689999123Xa.pdf
Prot.SciS096183689999123Xa.pdfGröße: 307.22 KBDownloads: 317
Datum
1999
Autor:innen
Wiener, Michael C.
Tamm, Lukas K.
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Protein Science. 1999, 8(10), pp. 2065-2071. ISSN 0961-8368. eISSN 1469-896X. Available under: doi: 10.1110/ps.8.10.2065
Zusammenfassung

Outer membrane protein A (OmpA) of Escherichia coli is a β-barrel membrane protein that unfolds in 8 M urea to a random coil. OmpA refolds upon urea dilution in the presence of certain detergents or lipids. To examine the minimal requirements for secondary and tertiary structure formation in β-barrel membrane proteins, folding of OmpA was studied as a function of the hydrophobic chain length, the chemical structure of the polar headgroup, and the concentration of a large array of amphiphiles. OmpA folded in the presence of detergents only above a critical minimal chain length of the apolar chain as determined by circular dichroism spectroscopy and a SDS-PAGE assay that measures tertiary structure formation. Details of the chemical structure of the polar headgroup were unimportant for folding. The minimal chain length required for folding correlated with the critical micelle concentration in each detergent series. Therefore, OmpA requires preformed detergent micelles for folding and does not adsorb monomeric detergent to its perimeter after folding. Formation of secondary and tertiary structure is thermodynamically coupled and strictly dependent on the interaction with aggregated amphiphiles.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
β-barrel, critical micelle concentration, membrane protein folding, outer membrane protein A, porin
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690KLEINSCHMIDT, Jörg, Michael C. WIENER, Lukas K. TAMM, 1999. Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent. In: Protein Science. 1999, 8(10), pp. 2065-2071. ISSN 0961-8368. eISSN 1469-896X. Available under: doi: 10.1110/ps.8.10.2065
BibTex
@article{Kleinschmidt1999Outer-6881,
  year={1999},
  doi={10.1110/ps.8.10.2065},
  title={Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent},
  number={10},
  volume={8},
  issn={0961-8368},
  journal={Protein Science},
  pages={2065--2071},
  author={Kleinschmidt, Jörg and Wiener, Michael C. and Tamm, Lukas K.}
}
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/123456789/6881">
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Wiener, Michael C.</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6881"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:format>application/pdf</dc:format>
    <dcterms:bibliographicCitation>First publ. in: Protein Science 8 (1999), 10,  pp. 2065-2071</dcterms:bibliographicCitation>
    <dcterms:issued>1999</dcterms:issued>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:52Z</dc:date>
    <dc:contributor>Tamm, Lukas K.</dc:contributor>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dcterms:abstract xml:lang="eng">Outer membrane protein A (OmpA) of Escherichia coli is a β-barrel membrane protein that unfolds in 8 M urea to a random coil. OmpA refolds upon urea dilution in the presence of certain detergents or lipids. To examine the minimal requirements for secondary and tertiary structure formation in β-barrel membrane proteins, folding of OmpA was studied as a function of the hydrophobic chain length, the chemical structure of the polar headgroup, and the concentration of a large array of amphiphiles. OmpA folded in the presence of detergents only above a critical minimal chain length of the apolar chain as determined by circular dichroism spectroscopy and a SDS-PAGE assay that measures tertiary structure formation. Details of the chemical structure of the polar headgroup were unimportant for folding. The minimal chain length required for folding correlated with the critical micelle concentration in each detergent series. Therefore, OmpA requires preformed detergent micelles for folding and does not adsorb monomeric detergent to its perimeter after folding. Formation of secondary and tertiary structure is thermodynamically coupled and strictly dependent on the interaction with aggregated amphiphiles.</dcterms:abstract>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6881/1/Prot.SciS096183689999123Xa.pdf"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6881/1/Prot.SciS096183689999123Xa.pdf"/>
    <dc:contributor>Kleinschmidt, Jörg</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:52Z</dcterms:available>
    <dc:creator>Kleinschmidt, Jörg</dc:creator>
    <dc:language>eng</dc:language>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:creator>Tamm, Lukas K.</dc:creator>
    <dc:contributor>Wiener, Michael C.</dc:contributor>
    <dcterms:title>Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent</dcterms:title>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet
Diese Publikation teilen