Publikation: Characterization of Non-Covalent Complexes of Synthetic Peptides of RNA Polymerase Subunit σ70 From Chlamydia trachomatis with Protein G by nanoESI-MS
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
To investigate the molecular mimicry between human ribosomal protein L7 with 70-kDa sigma factor (σ70) of the RNA polymerase of Chlamydia trachomatis, the complexes of synthetic σ70 peptides, σ(264–286), and σ(245–294), with protein G were investigated using nanoelectrospray ionization mass spectrometry (nanoESI-MS). The σ70 peptides were synthesized in the laboratory, purified by high performance liquid chromatography (HPLC), and identified by MS. The characteristics of the complexes of σ70 peptides with protein G were investigated under different conditions. The stability of the complexes decreased with the increase of declustering potential and acidity, whereas the sequence of σ70 peptides might have an obvious effect on the complex formation. In summary, the complexes of σ70 peptides with protein G are specific non-covalent binding. It is the first study regarding the binding of σ70 with protein G. This study could provide helpful information for the elucidation of binding mechanism of protein interaction and understanding of molecular mimicry.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
MA, Li, Markus KOHLMANN, Michael PRZYBYLSKI, Shuying LIU, 2015. Characterization of Non-Covalent Complexes of Synthetic Peptides of RNA Polymerase Subunit σ70 From Chlamydia trachomatis with Protein G by nanoESI-MS. In: Journal of Liquid Chromatography & Related Technologies. 2015, 38(10), pp. 1026-1030. ISSN 0148-3919. eISSN 1520-572X. Available under: doi: 10.1080/10826076.2014.968661BibTex
@article{Ma2015Chara-31691, year={2015}, doi={10.1080/10826076.2014.968661}, title={Characterization of Non-Covalent Complexes of Synthetic Peptides of RNA Polymerase Subunit σ70 From Chlamydia trachomatis with Protein G by nanoESI-MS}, number={10}, volume={38}, issn={0148-3919}, journal={Journal of Liquid Chromatography & Related Technologies}, pages={1026--1030}, author={Ma, Li and Kohlmann, Markus and Przybylski, Michael and Liu, Shuying} }
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/123456789/31691"> <dc:contributor>Ma, Li</dc:contributor> <dcterms:title>Characterization of Non-Covalent Complexes of Synthetic Peptides of RNA Polymerase Subunit σ70 From Chlamydia trachomatis with Protein G by nanoESI-MS</dcterms:title> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-09-05T10:18:13Z</dc:date> <dc:language>eng</dc:language> <dc:creator>Liu, Shuying</dc:creator> <dc:creator>Przybylski, Michael</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <dcterms:abstract xml:lang="eng">To investigate the molecular mimicry between human ribosomal protein L7 with 70-kDa sigma factor (σ70) of the RNA polymerase of Chlamydia trachomatis, the complexes of synthetic σ70 peptides, σ(264–286), and σ(245–294), with protein G were investigated using nanoelectrospray ionization mass spectrometry (nanoESI-MS). The σ70 peptides were synthesized in the laboratory, purified by high performance liquid chromatography (HPLC), and identified by MS. The characteristics of the complexes of σ70 peptides with protein G were investigated under different conditions. The stability of the complexes decreased with the increase of declustering potential and acidity, whereas the sequence of σ70 peptides might have an obvious effect on the complex formation. In summary, the complexes of σ70 peptides with protein G are specific non-covalent binding. It is the first study regarding the binding of σ70 with protein G. This study could provide helpful information for the elucidation of binding mechanism of protein interaction and understanding of molecular mimicry.</dcterms:abstract> <dcterms:issued>2015</dcterms:issued> <dc:contributor>Liu, Shuying</dc:contributor> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Kohlmann, Markus</dc:contributor> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:creator>Ma, Li</dc:creator> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/31691"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-09-05T10:18:13Z</dcterms:available> <dc:contributor>Przybylski, Michael</dc:contributor> <dc:creator>Kohlmann, Markus</dc:creator> </rdf:Description> </rdf:RDF>