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Differentiation of compact and extended conformations of di-ubiquitin conjugates with lysine-specific isopeptide linkages by ion mobility-mass spectrometry

Differentiation of compact and extended conformations of di-ubiquitin conjugates with lysine-specific isopeptide linkages by ion mobility-mass spectrometry

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JUNG, Ji Eun, Nicholas A. PIERSON, Andreas MARQUARDT, Martin SCHEFFNER, Michael PRZYBYLSKI, David E. CLEMMER, 2011. Differentiation of compact and extended conformations of di-ubiquitin conjugates with lysine-specific isopeptide linkages by ion mobility-mass spectrometry. In: Journal of The American Society for Mass Spectrometry. 22(8), pp. 1463-1471. ISSN 1044-0305. eISSN 1879-1123

@article{Jung2011-08Diffe-16762, title={Differentiation of compact and extended conformations of di-ubiquitin conjugates with lysine-specific isopeptide linkages by ion mobility-mass spectrometry}, year={2011}, doi={10.1007/s13361-011-0158-0}, number={8}, volume={22}, issn={1044-0305}, journal={Journal of The American Society for Mass Spectrometry}, pages={1463--1471}, author={Jung, Ji Eun and Pierson, Nicholas A. and Marquardt, Andreas and Scheffner, Martin and Przybylski, Michael and Clemmer, David E.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/16762"> <dc:language>eng</dc:language> <dcterms:bibliographicCitation>First publ. in: Journal of The American Society for Mass Spectrometry ; 22 (2011), 8. - S. 1463-1471</dcterms:bibliographicCitation> <dc:creator>Clemmer, David E.</dc:creator> <dc:creator>Przybylski, Michael</dc:creator> <dc:contributor>Marquardt, Andreas</dc:contributor> <dc:contributor>Clemmer, David E.</dc:contributor> <dc:creator>Scheffner, Martin</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/16762"/> <dc:contributor>Przybylski, Michael</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:creator>Marquardt, Andreas</dc:creator> <dc:contributor>Jung, Ji Eun</dc:contributor> <dcterms:title>Differentiation of compact and extended conformations of di-ubiquitin conjugates with lysine-specific isopeptide linkages by ion mobility-mass spectrometry</dcterms:title> <dc:contributor>Pierson, Nicholas A.</dc:contributor> <dcterms:issued>2011-08</dcterms:issued> <dc:creator>Jung, Ji Eun</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-07-31T22:25:05Z</dcterms:available> <dc:creator>Pierson, Nicholas A.</dc:creator> <dcterms:abstract xml:lang="eng">Modification of ubiquitin, a key cellular regulatory polypeptide of 76 amino acids, to polyubiquitin conjugates by lysine-specific isopeptide linkage at one of its seven lysine residues has been recognized as a central pathway determining its biochemical properties and cellular functions. Structural details and differences of distinct lysine-isopeptidyl ubiquitin conjugates that reflect their different functions and reactivities, however, are only partially understood. Ion mobility spectrometry (IMS) combined with mass spectrometry (MS) has recently emerged as a powerful tool for probing conformations and topology involved in protein interactions by an electric field-driven separation of polypeptide ions through a drift gas. Here we report the conformational characterization and differentiation of Lys63- and Lys48-linked ubiquitin conjugates by IMS-MS. Lys63- and Lys48-linked di-ubiquitin conjugates were prepared by recombinant bacterial expression and by chemical synthesis using a specific chemical ligation strategy, and characterized by high-resolution Fourier transform ion cyclotron resonance mass spectrometry, circular dichroism spectroscopy, and molecular modeling. IMS-MS was found to be an effective tool for the identification of structural differences of ubiquitin complexes in the gas phase. The comparison of collision cross-sections of Lys63- and Lys48-linked di-ubiquitin conjugates showed a more elongated conformation of Lys63-linked di-ubiquitin. In contrast, the Lys48-linked di-ubiquitin conjugate showed a more compact conformation. The IMS-MS results are consistent with published structural data and a comparative molecular modeling study of the Lys63- and Lys48-linked conjugates. The results presented here suggest IMS techniques can provide information that complements MS measurements in differentiating higher-order polyubiquitins and other isomeric protein linkages.</dcterms:abstract> <dc:contributor>Scheffner, Martin</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-11-16T08:42:06Z</dc:date> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

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