Journal article:
Time-resolved temperature-jump infrared spectroscopy of peptides with well-defined secondary structure : a Trpzip beta-hairpin variant as an example

No Thumbnail Available
Files
There are no files associated with this item.
Date
2008
Editors
Krejtschi, Carsten
Huang, Rong
relationships.isEditorOf
Contact
Journal ISSN
Electronic ISSN
ISBN
Bibliographical data
Publisher
Series
URI (citable link)
ArXiv-ID
International patent number
Link to the license
Project
EU project number
Open Access publication
Collections
Restricted until
Title in another language
Research Projects
Organizational Units
Journal Issue
Publication type
Journal article
Publication status
Abstract
Peptide folding dynamics were studied by time-resolved infrared spectroscopy after initiation with a nanosecond laser-excited temperature-jump. Relaxation kinetics are monitored using amide I′ absorption changes following rapid heating of the solvent by a Raman shifted Nd:YAG laser pulse. Lead salt laser diodes provide a tuneable IR source in the amide I′ region between 1600 cm−1 and 1700 cm−1 for probing structural unfolding at single wavelengths. The probe wavelengths are selected by using FTIR measurements that have been performed under thermal equilibrium conditions and indicate the amide I′ wavenumbers with the most significant absorption changes. Temperature-dependent spectral changes of water were separated from the spectral variation due to structural changes of the peptide, both in the equilibrium measurements and in the kinetic T-jump data. Polyglutamic acid has been used as a test system to demonstrate the capability of our instrument for acquiring microsecond peptide dynamics. In this work, we studied the relaxation dynamics of a 12-mer tryptophan zipper (Trpzip) peptide, a Trpzip2 variant, that adopts a stable β-hairpin structure in aqueous solution. Rate constants are a few microseconds depending on the sample temperature and are compared with published data indicating characteristics between those of Trpzip1 and Trpzip2.
Summary in another language
Subject (DDC)
540 Chemistry
Keywords
Peptide dynamics , Infrared spectroscopy , Temperature-jump , β-Hairpin
Published in
Vibrational Spectroscopy ; 48 (2008), 1. - pp. 1-7. - ISSN 0924-2031
Conference
Review
undefined / . - undefined, undefined. - (undefined; undefined)
Cite This
ISO 690KREJTSCHI, Carsten, Rong HUANG, Tim KEIDERLING, Karin HAUSER, 2008. Time-resolved temperature-jump infrared spectroscopy of peptides with well-defined secondary structure : a Trpzip beta-hairpin variant as an example. In: Vibrational Spectroscopy. 48(1), pp. 1-7. ISSN 0924-2031. Available under: doi: 10.1016/j.vibspec.2008.01.008
BibTex
@article{Krejtschi2008Timer-17544,
  year={2008},
  doi={10.1016/j.vibspec.2008.01.008},
  title={Time-resolved temperature-jump infrared spectroscopy of peptides with well-defined secondary structure : a Trpzip beta-hairpin variant as an example},
  number={1},
  volume={48},
  issn={0924-2031},
  journal={Vibrational Spectroscopy},
  pages={1--7},
  author={Krejtschi, Carsten and Huang, Rong and Keiderling, Tim and Hauser, Karin},
  note={Papers presented at the 4th international conference on advanced vibrational spectroscopy, Corfu, Greece, 10-15 june 2007 - part I}
}
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/123456789/17544">
    <dc:contributor>Hauser, Karin</dc:contributor>
    <dc:creator>Krejtschi, Carsten</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/17544"/>
    <dc:contributor>Keiderling, Tim</dc:contributor>
    <dc:contributor>Huang, Rong</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-26T15:37:24Z</dc:date>
    <dcterms:bibliographicCitation>Vibrational Spectroscopy ; 48 (2008), 1. - S. 1-7</dcterms:bibliographicCitation>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Hauser, Karin</dc:creator>
    <dc:creator>Huang, Rong</dc:creator>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:abstract xml:lang="eng">Peptide folding dynamics were studied by time-resolved infrared spectroscopy after initiation with a nanosecond laser-excited temperature-jump. Relaxation kinetics are monitored using amide I′ absorption changes following rapid heating of the solvent by a Raman shifted Nd:YAG laser pulse. Lead salt laser diodes provide a tuneable IR source in the amide I′ region between 1600 cm−1 and 1700 cm−1 for probing structural unfolding at single wavelengths. The probe wavelengths are selected by using FTIR measurements that have been performed under thermal equilibrium conditions and indicate the amide I′ wavenumbers with the most significant absorption changes. Temperature-dependent spectral changes of water were separated from the spectral variation due to structural changes of the peptide, both in the equilibrium measurements and in the kinetic T-jump data. Polyglutamic acid has been used as a test system to demonstrate the capability of our instrument for acquiring microsecond peptide dynamics. In this work, we studied the relaxation dynamics of a 12-mer tryptophan zipper (Trpzip) peptide, a Trpzip2 variant, that adopts a stable β-hairpin structure in aqueous solution. Rate constants are a few microseconds depending on the sample temperature and are compared with published data indicating characteristics between those of Trpzip1 and Trpzip2.</dcterms:abstract>
    <dc:rights>terms-of-use</dc:rights>
    <dc:language>eng</dc:language>
    <dcterms:title>Time-resolved temperature-jump infrared spectroscopy of peptides with well-defined secondary structure : a Trpzip beta-hairpin variant as an example</dcterms:title>
    <dc:creator>Keiderling, Tim</dc:creator>
    <dc:contributor>Krejtschi, Carsten</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-26T15:37:24Z</dcterms:available>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:issued>2008</dcterms:issued>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
  </rdf:Description>
</rdf:RDF>
Internal note
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Contact
URL of original publication
Test date of URL
Examination date of dissertation
Method of financing
Comment on publication
Papers presented at the 4th international conference on advanced vibrational spectroscopy, Corfu, Greece, 10-15 june 2007 - part I
Alliance license
Corresponding Authors der Uni Konstanz vorhanden
International Co-Authors
Bibliography of Konstanz
No
Refereed
Link to research data
Description of supplementary data