Publikation:

Time-Resolved Temperature-Jump Ir-Measurements on Beta-Hairpin Peptides with Alternate Cross-Strand Interactions

Lade...
Vorschaubild

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2014

Autor:innen

Wu, Ling
Keiderling, Timothy A.

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Biophysical Journal. 2014, 106(2), pp. 52a. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2013.11.370

Zusammenfassung

The formation of β-sheets plays an important role in protein folding. We studied the folding dynamics of tryptophan zipper (Trpzip) peptides being ideal simple model systems of β-hairpins stabilized by the hydrophobic interactions of two cross-strand Trp-Trp pairs. Rapid heating of the solvent is induced by a Raman-shifted Nd:YAG pulse (ΔT ∼ 10°C in 10 ns) and ns-to-µs peptide dynamics were monitored at single wavelengths using a quantum cascade laser tunable in the amide I region. Our isotope-edited kinetics support a multistate dynamic behavior being consistent with a hydrophobic collapse hypothesis for the folding process of Trpzip2 β-hairpin variants. In order to analyze hydrophobic interactions, the tryptophans in the Trpzip2 sequence (SWTWENGKWTWK-NH2) were replaced pairwise by either valines or tyrosines. Equilibrium CD and FTIR measurements show lower transition temperatures for all mutants. While the Trp-Trp stabilized peptides have different relaxation rates for the loss of sheet and gain of disordered structure, our mutant studies indicate that the aromatic substitution of Trp→Tyr results in kinetics being faster than for Trpzip2, but essentially the same for the sheet and disordered components, with similar activation energies. However with Val substitutions, different relaxation kinetics were found. Our time-resolved temperature-jump measurements reveal the impact of cross-strand interactions on the folding mechanism of peptides, in particular illustrate different effects of hydrophobic versus aromatic interactions on stability and dynamics of structure formation.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690POPP, Alexander, Ling WU, Timothy A. KEIDERLING, Karin HAUSER, 2014. Time-Resolved Temperature-Jump Ir-Measurements on Beta-Hairpin Peptides with Alternate Cross-Strand Interactions. In: Biophysical Journal. 2014, 106(2), pp. 52a. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2013.11.370
BibTex
@article{Popp2014TimeR-28662,
  year={2014},
  doi={10.1016/j.bpj.2013.11.370},
  title={Time-Resolved Temperature-Jump Ir-Measurements on Beta-Hairpin Peptides with Alternate Cross-Strand Interactions},
  number={2},
  volume={106},
  issn={0006-3495},
  journal={Biophysical Journal},
  author={Popp, Alexander and Wu, Ling and Keiderling, Timothy A. 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/123456789/28662">
    <dcterms:bibliographicCitation>Biophysical journal ; 106 (2014), 2 (Supplement 1). - S. 52a</dcterms:bibliographicCitation>
    <dcterms:issued>2014</dcterms:issued>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:contributor>Wu, Ling</dc:contributor>
    <dc:contributor>Keiderling, Timothy A.</dc:contributor>
    <dcterms:title>Time-Resolved Temperature-Jump Ir-Measurements on Beta-Hairpin Peptides with Alternate Cross-Strand Interactions</dcterms:title>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:abstract xml:lang="eng">The formation of β-sheets plays an important role in protein folding. We studied the folding dynamics of tryptophan zipper (Trpzip) peptides being ideal simple model systems of β-hairpins stabilized by the hydrophobic interactions of two cross-strand Trp-Trp pairs. Rapid heating of the solvent is induced by a Raman-shifted Nd:YAG pulse (ΔT ∼ 10°C in 10 ns) and ns-to-µs peptide dynamics were monitored at single wavelengths using a quantum cascade laser tunable in the amide I region. Our isotope-edited kinetics support a multistate dynamic behavior being consistent with a hydrophobic collapse hypothesis for the folding process of Trpzip2 β-hairpin variants. In order to analyze hydrophobic interactions, the tryptophans in the Trpzip2 sequence (SWTWENGKWTWK-NH2) were replaced pairwise by either valines or tyrosines. Equilibrium CD and FTIR measurements show lower transition temperatures for all mutants. While the Trp-Trp stabilized peptides have different relaxation rates for the loss of sheet and gain of disordered structure, our mutant studies indicate that the aromatic substitution of Trp→Tyr results in kinetics being faster than for Trpzip2, but essentially the same for the sheet and disordered components, with similar activation energies. However with Val substitutions, different relaxation kinetics were found. Our time-resolved temperature-jump measurements reveal the impact of cross-strand interactions on the folding mechanism of peptides, in particular illustrate different effects of hydrophobic versus aromatic interactions on stability and dynamics of structure formation.</dcterms:abstract>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/28662"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2014-08-13T15:21:52Z</dc:date>
    <dc:creator>Wu, Ling</dc:creator>
    <dc:contributor>Hauser, Karin</dc:contributor>
    <dc:rights>terms-of-use</dc:rights>
    <dc:creator>Popp, Alexander</dc:creator>
    <dc:creator>Hauser, Karin</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:contributor>Popp, Alexander</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2014-08-13T15:21:52Z</dcterms:available>
    <dc:creator>Keiderling, Timothy A.</dc:creator>
    <dc:language>eng</dc:language>
  </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