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Approaches to the characterisation of tertiary and supramolecular protein structures by combination of protein chemistry and mass spectometry

Approaches to the characterisation of tertiary and supramolecular protein structures by combination of protein chemistry and mass spectometry

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PRZYBYLSKI, Michael, Volker SCHNAIBLE, Jürgen KAST, S. BÜHLER, J. MICHELS, Andreas WATTENBERG, Thilo FLIGGE, Doris FORST, Kay DIEDERICHS, Uwe NESTEL, Kornelius ZETH, Michael O. GLOCKER, Wolfram WELTE, 1998. Approaches to the characterisation of tertiary and supramolecular protein structures by combination of protein chemistry and mass spectometry. In: ENS, Werner, ed., Kenneth G. STANDING, ed., Igor V. CHERNUSHEVICH, ed.. New Methods for the Study of Biomolecular Complexes. Dordrecht:Springer Netherlands, pp. 17-43. ISBN 978-90-481-5017-5

@inproceedings{Przybylski1998Appro-21176, title={Approaches to the characterisation of tertiary and supramolecular protein structures by combination of protein chemistry and mass spectometry}, year={1998}, doi={10.1007/978-94-015-9046-4_2}, isbn={978-90-481-5017-5}, address={Dordrecht}, publisher={Springer Netherlands}, booktitle={New Methods for the Study of Biomolecular Complexes}, pages={17--43}, editor={Ens, Werner and Standing, Kenneth G. and Chernushevich, Igor V.}, author={Przybylski, Michael and Schnaible, Volker and Kast, Jürgen and Bühler, S. and Michels, J. and Wattenberg, Andreas and Fligge, Thilo and Forst, Doris and Diederichs, Kay and Nestel, Uwe and Zeth, Kornelius and Glocker, Michael O. and Welte, Wolfram} }

<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/123456789/21176"> <dc:creator>Wattenberg, Andreas</dc:creator> <dc:contributor>Fligge, Thilo</dc:contributor> <dc:creator>Michels, J.</dc:creator> <dc:contributor>Kast, Jürgen</dc:contributor> <dc:creator>Glocker, Michael O.</dc:creator> <dc:creator>Forst, Doris</dc:creator> <dc:creator>Diederichs, Kay</dc:creator> <dc:contributor>Michels, J.</dc:contributor> <dc:creator>Welte, Wolfram</dc:creator> <dc:creator>Bühler, S.</dc:creator> <dc:rights>deposit-license</dc:rights> <dcterms:bibliographicCitation>New methods for the study of biomolecular complexes : [proceedings of the NATO Advanced Research Workshop on New Methods for the Study of Molecular Aggregates, The Lodge at Kananaskis Village, Alberta, Canada, 16-20 June 1996] / edited by W. Ens, K. G. Standing and I. V. Chernushevich. - Dordrecht [u.a.] : Kluwer Academic, 1998. - S. 17-43. - ISBN 0-7923-5003-0</dcterms:bibliographicCitation> <dc:contributor>Zeth, Kornelius</dc:contributor> <dc:creator>Fligge, Thilo</dc:creator> <dc:contributor>Wattenberg, Andreas</dc:contributor> <dc:contributor>Bühler, S.</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-01-29T10:25:47Z</dc:date> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/21176"/> <dc:contributor>Przybylski, Michael</dc:contributor> <dc:contributor>Glocker, Michael O.</dc:contributor> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:creator>Zeth, Kornelius</dc:creator> <dc:contributor>Welte, Wolfram</dc:contributor> <dcterms:title>Approaches to the characterisation of tertiary and supramolecular protein structures by combination of protein chemistry and mass spectometry</dcterms:title> <dcterms:abstract xml:lang="eng">Soft-ionisation methods, particularly e!ectrospray (ESI) and matrix-assisted laser desorption (MALDI) have enabled a breakthrough in the mass spectrometric structure analysis of proteins. Whereas ESI-MS provides direct information about solution structures and non-covalent interactions, the combination of mass spectrometry with structure-specific protein chemistry is emerging presently as a powerful tool for characterising tertiary structures and structure-function relations. Recent developments of chemical modification reactions are summarised which are suitable to the mass spectrometric analysis of reactive sites, surface topology and antigenic determinants in protein-tertiary structures, and can be efficiently employed in x-ray crystallographic structure determinations. Applications to the structure elucidation, and functional characterisation of porin-channel proteins and to leucine zipper protein-nucleotide complexes illustrate their efficiency in the analysis of two most important topics of structural biology, molecular recognition structures and biomacromolecular interaction.</dcterms:abstract> <dc:contributor>Schnaible, Volker</dc:contributor> <dc:contributor>Forst, Doris</dc:contributor> <dc:contributor>Nestel, Uwe</dc:contributor> <dc:creator>Kast, Jürgen</dc:creator> <dc:language>eng</dc:language> <dc:creator>Nestel, Uwe</dc:creator> <dc:creator>Przybylski, Michael</dc:creator> <dc:creator>Schnaible, Volker</dc:creator> <dcterms:issued>1998</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-01-29T10:25:47Z</dcterms:available> <dc:contributor>Diederichs, Kay</dc:contributor> </rdf:Description> </rdf:RDF>

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