Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT-IR as a spectroscopic tool to study lipid-protein interaction
Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT-IR as a spectroscopic tool to study lipid-protein interaction
Lade...
Datum
2005
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
eISSN
item.preview.dc.identifier.isbn
Bibliografische Daten
Verlag
Schriftenreihe
URI (zitierfähiger Link)
DOI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
EU-Projektnummer
Projekt
Open Access-Veröffentlichung
Sammlungen
Titel in einer weiteren Sprache
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Erschienen in
FEBS Letters ; 579 (2005), 12. - S. 2546-2550. - ISSN 0014-5793
Zusammenfassung
Abstract Lipid protein interactions play a key role in the stability and function of various membrane proteins. Earlier we have reported the extreme thermal stability of porin from Paracoccus denitrificans reconstituted into liposomes. Here, we used Fourier transform infrared spectroscopy for a label free analysis of the global secondary structural changes and local changes in the tyrosine microenvironment. Our results show that a mixed lipid system (non-uniform bilayer) optimizes the thermal stability of porin as compared to the porin in pure lipids (uniform bilayer) or detergent micelles. This is in line with the fact that the bacterial outer membrane is a dynamic system made up of lipids of varying chain lengths, head groups and the barrel wall height contacting the membrane is uneven.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
540 Chemie
Schlagwörter
Porin,Membrane protein stability,Lipid-protein interaction,Fourier transform infrared spectroscopy
Konferenz
Rezension
undefined / . - undefined, undefined. - (undefined; undefined)
Zitieren
ISO 690
SUKUMARAN, Suja, Karin HAUSER, Annette RAUSCHER, Werner MÄNTELE, 2005. Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT-IR as a spectroscopic tool to study lipid-protein interaction. In: FEBS Letters. 579(12), pp. 2546-2550. ISSN 0014-5793. Available under: doi: 10.1016/j.febslet.2005.03.059BibTex
@article{Sukumaran2005-05-09Therm-17552, year={2005}, doi={10.1016/j.febslet.2005.03.059}, title={Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT-IR as a spectroscopic tool to study lipid-protein interaction}, number={12}, volume={579}, issn={0014-5793}, journal={FEBS Letters}, pages={2546--2550}, author={Sukumaran, Suja and Hauser, Karin and Rauscher, Annette and Mäntele, Werner} }
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/123456789/17552"> <dc:creator>Sukumaran, Suja</dc:creator> <dc:rights>terms-of-use</dc:rights> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Rauscher, Annette</dc:creator> <dcterms:issued>2005-05-09</dcterms:issued> <dc:contributor>Rauscher, Annette</dc:contributor> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:language>eng</dc:language> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-04-04T07:19:08Z</dcterms:available> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-04-04T07:19:08Z</dc:date> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/17552/2/hauser_thermal.pdf"/> <dc:contributor>Sukumaran, Suja</dc:contributor> <dc:contributor>Mäntele, Werner</dc:contributor> <dc:creator>Hauser, Karin</dc:creator> <dcterms:bibliographicCitation>First publ. in: FEBS Letters ; 579 (2005), 12. - S. 2546-2550</dcterms:bibliographicCitation> <dc:contributor>Hauser, Karin</dc:contributor> <dc:creator>Mäntele, Werner</dc:creator> <dcterms:title>Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT-IR as a spectroscopic tool to study lipid-protein interaction</dcterms:title> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/17552"/> <dcterms:abstract xml:lang="eng">Abstract Lipid protein interactions play a key role in the stability and function of various membrane proteins. Earlier we have reported the extreme thermal stability of porin from Paracoccus denitrificans reconstituted into liposomes. Here, we used Fourier transform infrared spectroscopy for a label free analysis of the global secondary structural changes and local changes in the tyrosine microenvironment. Our results show that a mixed lipid system (non-uniform bilayer) optimizes the thermal stability of porin as compared to the porin in pure lipids (uniform bilayer) or detergent micelles. This is in line with the fact that the bacterial outer membrane is a dynamic system made up of lipids of varying chain lengths, head groups and the barrel wall height contacting the membrane is uneven.</dcterms:abstract> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/17552/2/hauser_thermal.pdf"/> </rdf:Description> </rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein