Site-specific folding dynamics of isotopically labeled peptides studied by time-resolved infrared-spectroscopy

Lade...
Vorschaubild
Dateien
Zu diesem Dokument gibt es keine Dateien.
Datum
2009
Autor:innen
Wu, Ling
Huang, Rong
Krejtschi, Carsten
Keiderling, Timothy A.
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
ArXiv-ID
Internationale Patentnummer
EU-Projektnummer
DFG-Projektnummer
Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Biophysical Journal. 2009, 96(3), pp. 73a. ISSN 0006-3495. Available under: doi: 10.1016/j.bpj.2008.12.275
Zusammenfassung

Peptides with well-defined secondary structure are ideal model systems for study of protein folding dynamics for specific, unique structures. IR techniques provide the necessary time resolution as well as have structural sensitivity, which arises from coupling of sequential residues, normally evidenced as a splitting or frequency shift of the amide centered transitions. The amide I region, mainly the C¼O stretching vibrations of the polypeptide backbone, is the prime target band for secondary structure. Isotopic labeling of individual amide 13C¼O groups can induce site-specific frequency shifts and provide insight into local structure. A nanosecond laser is used to excite the solvent and induce a fast temperature jump (~10 C), and relaxation dynamics are probed with a diode laser tuned to selected, structurally sensitive wavenumbers across the amide I absorption. Site-specific dynamics have been monitored for the thermal unfolding of an isotopically labeled beta-hairpin peptide, a 12-mer tryptophan zipper peptide, which has a hydrophobic core formed by four Trp residues, by use of cross-strand coupled 13C¼O labeled variants [1]. Data for single labeled peptides provided a control. Mutants of this sequence with just two Trp residues were introduced to destabilize the hairpin selectively near the termini or near the turn. Differences in kinetic behavior have been found for the loss of beta-strand and the gain of disordered structure. The isotope-edited kinetics vary with labeling position along the hairpin backbone and the mutations show consistent patterns depending on position. Our data supports a multistate folding mechanism for this hairpin structure. Similarly obtained data for other model peptides provide useful basis for interpretation of the observations.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
540 Chemie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690WU, Ling, Rong HUANG, Karin HAUSER, Carsten KREJTSCHI, Timothy A. KEIDERLING, 2009. Site-specific folding dynamics of isotopically labeled peptides studied by time-resolved infrared-spectroscopy. In: Biophysical Journal. 2009, 96(3), pp. 73a. ISSN 0006-3495. Available under: doi: 10.1016/j.bpj.2008.12.275
BibTex
@article{Wu2009Sites-17531,
  year={2009},
  doi={10.1016/j.bpj.2008.12.275},
  title={Site-specific folding dynamics of isotopically labeled peptides studied by time-resolved infrared-spectroscopy},
  number={3},
  volume={96},
  issn={0006-3495},
  journal={Biophysical Journal},
  author={Wu, Ling and Huang, Rong and Hauser, Karin and Krejtschi, Carsten and Keiderling, Timothy A.}
}
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/123456789/17531">
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:language>eng</dc:language>
    <dc:contributor>Huang, Rong</dc:contributor>
    <dc:contributor>Keiderling, Timothy A.</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:contributor>Wu, Ling</dc:contributor>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:creator>Krejtschi, Carsten</dc:creator>
    <dc:rights>terms-of-use</dc:rights>
    <dc:creator>Keiderling, Timothy A.</dc:creator>
    <dcterms:issued>2009</dcterms:issued>
    <dcterms:abstract xml:lang="eng">Peptides with well-defined secondary structure are ideal model systems for study of protein folding dynamics for specific, unique structures. IR techniques provide the necessary time resolution as well as have structural sensitivity, which arises from coupling of sequential residues, normally evidenced as a splitting or frequency shift of the amide centered transitions. The amide I region, mainly the C¼O stretching vibrations of the polypeptide backbone, is the prime target band for secondary structure. Isotopic labeling of individual amide 13C¼O groups can induce site-specific frequency shifts and provide insight into local structure. A nanosecond laser is used to excite the solvent and induce a fast temperature jump (~10 C), and relaxation dynamics are probed with a diode laser tuned to selected, structurally sensitive wavenumbers across the amide I absorption. Site-specific dynamics have been monitored for the thermal unfolding of an isotopically labeled beta-hairpin peptide, a 12-mer tryptophan zipper peptide, which has a hydrophobic core formed by four Trp residues, by use of cross-strand coupled 13C¼O labeled variants [1]. Data for single labeled peptides provided a control. Mutants of this sequence with just two Trp residues were introduced to destabilize the hairpin selectively near the termini or near the turn. Differences in kinetic behavior have been found for the loss of beta-strand and the gain of disordered structure. The isotope-edited kinetics vary with labeling position along the hairpin backbone and the mutations show consistent patterns depending on position. Our data supports a multistate folding mechanism for this hairpin structure. Similarly obtained data for other model peptides provide useful basis for interpretation of the observations.</dcterms:abstract>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-18T11:03:18Z</dcterms:available>
    <dcterms:bibliographicCitation>Publ. in: Biophysical Journal ; 96 (2009), 3. - S. 73a</dcterms:bibliographicCitation>
    <dc:contributor>Hauser, Karin</dc:contributor>
    <dcterms:title>Site-specific folding dynamics of isotopically labeled peptides studied by time-resolved infrared-spectroscopy</dcterms:title>
    <dc:creator>Hauser, Karin</dc:creator>
    <dc:contributor>Krejtschi, Carsten</dc:contributor>
    <dc:creator>Wu, Ling</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/17531"/>
    <dc:creator>Huang, Rong</dc:creator>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-18T11:03:18Z</dc:date>
  </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
Nein
Begutachtet