Three-Strand β-Sheet Peptide Models : IR, VCD and ECD SPECTRA, T-Jump Dynamics and NMR Structures Support MD and DFT Simulatations
| Publikationstyp: | Zeitschriftenartikel |
| Publikationsstatus: | Published |
| Autor/innen: | Keiderling, Timothy A.; Chi, Heng; McElheny, Dan; Walker, Allen; Scheerer, David; Hauser, Karin |
| Erscheinungsjahr: | 2017 |
| Erschienen in: | Biophysical Journal ; 112 (2017), 3, Supplement 1. - S. 195a. - ISSN 0006-3495. - eISSN 1542-0086 |
| DOI (zitierfähiger Link): | https://dx.doi.org/10.1016/j.bpj.2016.11.1082 |
| Zusammenfassung: |
Spectroscopic studies of peptide β-sheets is complicated by their having many forms (parallel vs. anti-parallel, twisted or flat, in and out of register) and being subject to aggregation so that the molecular state being studied experimentally becomes obscure and thus very difficult to model theoretically. We have used simple hairpin models (strand-turn-strand) to develop monomer structures that have cross-strand anti-parallel H-bonding characteristic of sheets, however these strands are also solvated on each edge.
|
| Fachgebiet (DDC): | 540 Chemie |
| Universitätsbibliographie: | Ja |
Zitieren
Dateien zu dieser Ressource
| Dateien | Größe | Format | Anzeige |
|---|---|---|---|
|
Zu diesem Dokument gibt es keine Dateien. |
|||
KEIDERLING, Timothy A., Heng CHI, Dan MCELHENY, Allen WALKER, David SCHEERER, Karin HAUSER, 2017. Three-Strand β-Sheet Peptide Models : IR, VCD and ECD SPECTRA, T-Jump Dynamics and NMR Structures Support MD and DFT Simulatations. In: Biophysical Journal. 112(3, Supplement 1), pp. 195a. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2016.11.1082
@article{Keiderling2017-02Three-38481, title={Three-Strand β-Sheet Peptide Models : IR, VCD and ECD SPECTRA, T-Jump Dynamics and NMR Structures Support MD and DFT Simulatations}, year={2017}, doi={10.1016/j.bpj.2016.11.1082}, number={3, Supplement 1}, volume={112}, issn={0006-3495}, journal={Biophysical Journal}, author={Keiderling, Timothy A. and Chi, Heng and McElheny, Dan and Walker, Allen and Scheerer, David and Hauser, Karin} }
<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/rdf/resource/123456789/38481"> <dc:creator>McElheny, Dan</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38481"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-12T10:55:16Z</dcterms:available> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:contributor>Scheerer, David</dc:contributor> <dc:contributor>McElheny, Dan</dc:contributor> <dcterms:title>Three-Strand β-Sheet Peptide Models : IR, VCD and ECD SPECTRA, T-Jump Dynamics and NMR Structures Support MD and DFT Simulatations</dcterms:title> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-12T10:55:16Z</dc:date> <dc:creator>Hauser, Karin</dc:creator> <dc:contributor>Walker, Allen</dc:contributor> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <dc:contributor>Hauser, Karin</dc:contributor> <dc:creator>Chi, Heng</dc:creator> <dcterms:issued>2017-02</dcterms:issued> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <dc:contributor>Keiderling, Timothy A.</dc:contributor> <dcterms:abstract xml:lang="eng">Spectroscopic studies of peptide β-sheets is complicated by their having many forms (parallel vs. anti-parallel, twisted or flat, in and out of register) and being subject to aggregation so that the molecular state being studied experimentally becomes obscure and thus very difficult to model theoretically. We have used simple hairpin models (strand-turn-strand) to develop monomer structures that have cross-strand anti-parallel H-bonding characteristic of sheets, however these strands are also solvated on each edge.</dcterms:abstract> <dc:language>eng</dc:language> <dc:contributor>Chi, Heng</dc:contributor> <dc:creator>Scheerer, David</dc:creator> <dc:creator>Walker, Allen</dc:creator> <dc:creator>Keiderling, Timothy A.</dc:creator> </rdf:Description> </rdf:RDF>
Das Dokument erscheint in:
KOPS Suche
Stöbern
Mein Benutzerkonto
