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Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline

Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline

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RODERER, Daniel, Rudi GLOCKSHUBER, Marina RUBINI, 2015. Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline. In: ChemBioChem. 16(15), pp. 2162-2166. ISSN 1439-4227. eISSN 1439-7633

@article{Roderer2015Accel-32629, title={Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline}, year={2015}, doi={10.1002/cbic.201500342}, number={15}, volume={16}, issn={1439-4227}, journal={ChemBioChem}, pages={2162--2166}, author={Roderer, Daniel and Glockshuber, Rudi and Rubini, Marina} }

<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/123456789/32629"> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/32629"/> <dc:creator>Glockshuber, Rudi</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-01-19T13:49:29Z</dcterms:available> <dcterms:abstract xml:lang="eng">The incorporation of the non-natural amino acids (4R)- and (4S)-fluoroproline (Flp) has been successfully used to improve protein stability, but little is known about their effect on protein folding kinetics. Here we analyzed the influence of (4R)- and (4S)-Flp on the rate-limiting trans-to-cis isomerization of the Ile75-Pro76 peptide bond in the folding of Escherichia coli thioredoxin (Trx). While (4R)-Flp at position 76 had essentially no effect on the isomerization rate in the context of the intact tertiary structure, (4S)-Flp accelerated the folding reaction ninefold. Similarly, tenfold faster trans-to-cis isomerization of Ile75-(4S)-Flp76 relative to Ile75-Pro76 was observed in the unfolded state of Trx. Our results show that the replacement of cis prolines by non-natural proline analogues can be used for modulating the folding rates of proteins with cis prolyl-peptide bonds in the native state.</dcterms:abstract> <dcterms:title>Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline</dcterms:title> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-01-19T13:49:29Z</dc:date> <dc:creator>Rubini, Marina</dc:creator> <dc:contributor>Rubini, Marina</dc:contributor> <dc:language>eng</dc:language> <dc:creator>Roderer, Daniel</dc:creator> <dcterms:issued>2015</dcterms:issued> <dc:contributor>Glockshuber, Rudi</dc:contributor> <dc:contributor>Roderer, Daniel</dc:contributor> </rdf:Description> </rdf:RDF>

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