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Rational Design of Protein Stability : Effect of (2S,4R)-4-Fluoroproline on the Stability and Folding Pathway of Ubiquitin

Rational Design of Protein Stability : Effect of (2S,4R)-4-Fluoroproline on the Stability and Folding Pathway of Ubiquitin

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CRESPO, Maria D., Marina RUBINI, 2011. Rational Design of Protein Stability : Effect of (2S,4R)-4-Fluoroproline on the Stability and Folding Pathway of Ubiquitin. In: PLoS ONE. 6(5), e19425. eISSN 1932-6203

@article{Crespo2011Ratio-18902, title={Rational Design of Protein Stability : Effect of (2S,4R)-4-Fluoroproline on the Stability and Folding Pathway of Ubiquitin}, year={2011}, doi={10.1371/journal.pone.0019425}, number={5}, volume={6}, journal={PLoS ONE}, author={Crespo, Maria D. and Rubini, Marina}, note={Article Number: e19425} }

<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/123456789/18902"> <dc:rights>deposit-license</dc:rights> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:language>eng</dc:language> <dc:creator>Crespo, Maria D.</dc:creator> <dc:contributor>Rubini, Marina</dc:contributor> <dcterms:title>Rational Design of Protein Stability : Effect of (2S,4R)-4-Fluoroproline on the Stability and Folding Pathway of Ubiquitin</dcterms:title> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/18902"/> <dc:contributor>Crespo, Maria D.</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-04-04T09:15:02Z</dc:date> <dcterms:abstract>Many strategies have been employed to increase the conformational stability of proteins. The use of 4-substituted proline analogs capable to induce pre-organization in target proteins is an attractive tool to deliver an additional conformational stability without perturbing the overall protein structure. Both, peptides and proteins containing 4-fluorinated proline derivatives can be stabilized by forcing the pyrrolidine ring in its favored puckering conformation. The fluorinated pyrrolidine rings of proline can preferably stabilize either a C(γ)-exo or a C(γ)-endo ring pucker in dependence of proline chirality (4R/4S) in a complex protein structure. To examine whether this rational strategy can be generally used for protein stabilization, we have chosen human ubiquitin as a model protein which contains three proline residues displaying C(γ)-exo puckering.</dcterms:abstract> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-04-04T09:15:02Z</dcterms:available> <dc:creator>Rubini, Marina</dc:creator> <dcterms:bibliographicCitation>First publ. in: PLoS ONE ; 6 (2011), 5. - e19425</dcterms:bibliographicCitation> <dcterms:issued>2011</dcterms:issued> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

journal.pone.0019425crespo.pdf 125

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