Reversible dioxygen binding in solvent-free liquid myoglobin

Lade...
Vorschaubild
Dateien
Cölfen12.pdf
Cölfen12.pdfGröße: 2.08 MBDownloads: 340
Cölfen12 SI.pdf
Cölfen12 SI.pdfGröße: 2.03 MBDownloads: 94
Datum
2010
Autor:innen
Perriman, Adam W.
Brogan, Alex P. S.
Tsoureas, Nikolaos
Owen, Gareth R.
Mann, Stephen
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Nature Chemistry. 2010, 2(8), pp. 622-626. ISSN 1755-4330. eISSN 1755-4349. Available under: doi: 10.1038/nchem.700
Zusammenfassung

The ensemble of forces that stabilize protein structure and facilitate biological function are intimately linked with the ubiquitous aqueous environment of living systems. As a consequence, biomolecular activity is highly sensitive to the interplay of solvent–protein interactions, and deviation from the native conditions, for example by exposure to increased thermal energy or severe dehydration, results in denaturation and subsequent loss of function. Although certain enzymes can be extracted into non-aqueous solvents without significant loss of activity, there are no known examples of solvent-less (molten) liquids of functional metalloproteins. Here we describe the synthesis and properties of room-temperature solvent-free myoglobin liquids with near-native structure and reversible dioxygen binding ability equivalent to the haem protein under physiological conditions. The realization of room-temperature solvent-free myoglobin liquids with retained function presents novel challenges to existing theories on the role of solvent molecules in structural biology, and should offer new opportunities in protein-based nanoscience and bionanotechnology.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
540 Chemie
Schlagwörter
Biochemistry, Materials chemistry
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690PERRIMAN, Adam W., Alex P. S. BROGAN, Helmut CÖLFEN, Nikolaos TSOUREAS, Gareth R. OWEN, Stephen MANN, 2010. Reversible dioxygen binding in solvent-free liquid myoglobin. In: Nature Chemistry. 2010, 2(8), pp. 622-626. ISSN 1755-4330. eISSN 1755-4349. Available under: doi: 10.1038/nchem.700
BibTex
@article{Perriman2010Rever-13550,
  year={2010},
  doi={10.1038/nchem.700},
  title={Reversible dioxygen binding in solvent-free liquid myoglobin},
  number={8},
  volume={2},
  issn={1755-4330},
  journal={Nature Chemistry},
  pages={622--626},
  author={Perriman, Adam W. and Brogan, Alex P. S. and Cölfen, Helmut and Tsoureas, Nikolaos and Owen, Gareth R. and Mann, Stephen}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/13550">
    <dc:contributor>Brogan, Alex P. S.</dc:contributor>
    <dc:creator>Tsoureas, Nikolaos</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-30T23:25:13Z</dcterms:available>
    <dc:language>eng</dc:language>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-06-09T11:31:24Z</dc:date>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/13550/3/C%c3%b6lfen12%20SI.pdf"/>
    <dcterms:abstract xml:lang="eng">The ensemble of forces that stabilize protein structure and facilitate biological function are intimately linked with the ubiquitous aqueous environment of living systems. As a consequence, biomolecular activity is highly sensitive to the interplay of solvent–protein interactions, and deviation from the native conditions, for example by exposure to increased thermal energy or severe dehydration, results in denaturation and subsequent loss of function. Although certain enzymes can be extracted into non-aqueous solvents without significant loss of activity, there are no known examples of solvent-less (molten) liquids of functional metalloproteins. Here we describe the synthesis and properties of room-temperature solvent-free myoglobin liquids with near-native structure and reversible dioxygen binding ability equivalent to the haem protein under physiological conditions. The realization of room-temperature solvent-free myoglobin liquids with retained function presents novel challenges to existing theories on the role of solvent molecules in structural biology, and should offer new opportunities in protein-based nanoscience and bionanotechnology.</dcterms:abstract>
    <dc:contributor>Cölfen, Helmut</dc:contributor>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/13550/2/C%c3%b6lfen12.pdf"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/13550"/>
    <dc:contributor>Tsoureas, Nikolaos</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Cölfen, Helmut</dc:creator>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:contributor>Owen, Gareth R.</dc:contributor>
    <dc:contributor>Perriman, Adam W.</dc:contributor>
    <dc:contributor>Mann, Stephen</dc:contributor>
    <dcterms:issued>2010</dcterms:issued>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:creator>Mann, Stephen</dc:creator>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/13550/2/C%c3%b6lfen12.pdf"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/13550/3/C%c3%b6lfen12%20SI.pdf"/>
    <dc:creator>Brogan, Alex P. S.</dc:creator>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dcterms:title>Reversible dioxygen binding in solvent-free liquid myoglobin</dcterms:title>
    <dcterms:bibliographicCitation>First publ. in: Nature Chemistry 2 (2010), 8, pp. 622-626, doi:10.1038/nchem.700</dcterms:bibliographicCitation>
    <dc:creator>Perriman, Adam W.</dc:creator>
    <dc:creator>Owen, Gareth R.</dc:creator>
    <dc:rights>terms-of-use</dc:rights>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Diese Publikation teilen