Publikation:

Three-Strand β-Sheet Peptide Models : IR, VCD and ECD SPECTRA, T-Jump Dynamics and NMR Structures Support MD and DFT Simulatations

Vorschaubild

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2017

Autor:innen

Keiderling, Timothy A.
Chi, Heng
McElheny, Dan
Walker, Allen

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

URI (zitierfähiger Link)
DOI (zitierfähiger Link)
https://doi.org/10.1016/j.bpj.2016.11.1082
ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung

Sammlungen

Chemie: Publikationen
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Biophysical Journal. 2017, 112(3, Supplement 1), pp. 195a. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 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.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690KEIDERLING, 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. 2017, 112(3, Supplement 1), pp. 195a. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2016.11.1082
BibTex
@article{Keiderling2017-02Three-38481,
  year={2017},
  doi={10.1016/j.bpj.2016.11.1082},
  title={Three-Strand β-Sheet Peptide Models : IR, VCD and ECD SPECTRA, T-Jump Dynamics and NMR Structures Support MD and DFT Simulatations},
  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: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/123456789/38481">
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-12T10:55:16Z</dcterms:available>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38481"/>
    <dc:contributor>Hauser, Karin</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <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:creator>Scheerer, David</dc:creator>
    <dc:creator>McElheny, Dan</dc:creator>
    <dc:contributor>Scheerer, David</dc:contributor>
    <dc:contributor>McElheny, Dan</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-12T10:55:16Z</dc:date>
    <dc:creator>Keiderling, Timothy A.</dc:creator>
    <dc:contributor>Keiderling, Timothy A.</dc:contributor>
    <dc:language>eng</dc:language>
    <dc:contributor>Walker, Allen</dc:contributor>
    <dc:creator>Hauser, Karin</dc:creator>
    <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:creator>Walker, Allen</dc:creator>
    <dc:contributor>Chi, Heng</dc:contributor>
    <dc:creator>Chi, Heng</dc:creator>
    <dcterms:issued>2017-02</dcterms:issued>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
  </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