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(4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold : tertiary structure context dictates ring puckering

(4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold : tertiary structure context dictates ring puckering

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RUBINI, Marina, Martin SCHÄRER, Guido CAPITANI, Rudi GLOCKSHUBER, 2013. (4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold : tertiary structure context dictates ring puckering. In: ChemBioChem. 14(9), pp. 1053-1057. ISSN 1439-4227. eISSN 1439-7633

@article{Rubini2013-06-17(4R)--24514, title={(4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold : tertiary structure context dictates ring puckering}, year={2013}, doi={10.1002/cbic.201300178}, number={9}, volume={14}, issn={1439-4227}, journal={ChemBioChem}, pages={1053--1057}, author={Rubini, Marina and Schärer, Martin and Capitani, Guido and Glockshuber, Rudi} }

<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/123456789/24514"> <dc:language>eng</dc:language> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/24514"/> <dcterms:title>(4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold : tertiary structure context dictates ring puckering</dcterms:title> <dc:contributor>Capitani, Guido</dc:contributor> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:creator>Rubini, Marina</dc:creator> <dcterms:issued>2013-06-17</dcterms:issued> <dc:creator>Glockshuber, Rudi</dc:creator> <dc:creator>Schärer, Martin</dc:creator> <dc:creator>Capitani, Guido</dc:creator> <dcterms:abstract xml:lang="eng">Fine-tuning protein stability: The non-natural amino acids (2S,4R)- and (2S,4S)-fluoroproline modulate protein stability by biasing the proline ring pucker and the cis/trans equilibrium of prolyl peptide bonds. We incorporated both fluoroproline stereoisomers at the invariant cis-proline residue of the thioredoxin fold. The results show that tertiary structure context overrules the conformational preferences of fluoroprolines.</dcterms:abstract> <dc:contributor>Rubini, Marina</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:contributor>Glockshuber, Rudi</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-10-01T10:23:19Z</dcterms:available> <dcterms:bibliographicCitation>ChemBioChem ; 14 (2013), 9. - S. 1053-1057</dcterms:bibliographicCitation> <dc:contributor>Schärer, Martin</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-10-01T10:23:19Z</dc:date> </rdf:Description> </rdf:RDF>

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