Mass Spectrometric Analysis of Noncovalent Complexes Between Synthetic Peptides from Human Ribosomal Protein L7 and Protein G

No Thumbnail Available
Files
There are no files associated with this item.
Date
2015
Authors
Ma, Li
Kohlmann, Markus
Wochner, Michael
Krawinkel, Ulrich
Liu, Shuying
Editors
Contact
Journal ISSN
Electronic ISSN
ISBN
Bibliographical data
Publisher
Series
URI (citable link)
ArXiv-ID
International patent number
Link to the license
oops
EU project number
Project
Open Access publication
Collections
Restricted until
Title in another language
Research Projects
Organizational Units
Journal Issue
Publication type
Journal article
Publication status
Published in
Journal of Liquid Chromatography & Related Technologies ; 38 (2015), 10. - pp. 1007-1013. - ISSN 0148-3919. - eISSN 1520-572X
Abstract
In order to gain a comprehensive insight into the complexes of human ribosomal protein L7 with protein G in a certain degree, an investigation on the complexes of five synthetic L7 peptides, containing the basic-region-leucine-zipper (BZIP)-like domain (aa 15–49), with protein G was performed using nanoelectrospray ionization mass spectrometry (nanoESI-MS). Circular dichroism (CD) was used to characterize the secondary structures of L7 peptides. The characteristics of the complexes between L7 peptides and protein G were studied under various conditions, such as molar ratio of ligands, solvent condition, declustering potential, and peptide sequence. The stability of the complexes is found to decrease with increased declustering potential (>20 V), decreased pH (<5), increased pH (>5), while L7 peptide sequence had no obvious effect on the complex formation. Taken together, the complexes of L7 peptides with protein G are specific noncovalent binding with 1:1 stoichiometry. Because of the availability of synthetic L7 peptides, they might be used as baits to discover the binding partners of protein L7. Furthermore, the elaboration of the binding mechanisms of L7 peptides with protein G could benefit further application of protein G.
Summary in another language
Subject (DDC)
540 Chemistry
Keywords
electronspray ionization, L7 peptide, mass spectrometry, noncovalent complex, protein G, stability
Conference
Review
undefined / . - undefined, undefined. - (undefined; undefined)
Cite This
ISO 690MA, Li, Markus KOHLMANN, Michael WOCHNER, Ulrich KRAWINKEL, Michael PRZYBYLSKI, Shuying LIU, 2015. Mass Spectrometric Analysis of Noncovalent Complexes Between Synthetic Peptides from Human Ribosomal Protein L7 and Protein G. In: Journal of Liquid Chromatography & Related Technologies. 38(10), pp. 1007-1013. ISSN 0148-3919. eISSN 1520-572X. Available under: doi: 10.1080/10826076.2014.922475
BibTex
@article{Ma2015Spect-31101,
  year={2015},
  doi={10.1080/10826076.2014.922475},
  title={Mass Spectrometric Analysis of Noncovalent Complexes Between Synthetic Peptides from Human Ribosomal Protein L7 and Protein G},
  number={10},
  volume={38},
  issn={0148-3919},
  journal={Journal of Liquid Chromatography & Related Technologies},
  pages={1007--1013},
  author={Ma, Li and Kohlmann, Markus and Wochner, Michael and Krawinkel, Ulrich and Przybylski, Michael and Liu, Shuying}
}
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/123456789/31101">
    <dc:creator>Liu, Shuying</dc:creator>
    <dcterms:issued>2015</dcterms:issued>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-06-03T06:44:25Z</dc:date>
    <dc:creator>Kohlmann, Markus</dc:creator>
    <dc:contributor>Krawinkel, Ulrich</dc:contributor>
    <dc:creator>Wochner, Michael</dc:creator>
    <dc:creator>Przybylski, Michael</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-06-03T06:44:25Z</dcterms:available>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/31101"/>
    <dcterms:title>Mass Spectrometric Analysis of Noncovalent Complexes Between Synthetic Peptides from Human Ribosomal Protein L7 and Protein G</dcterms:title>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Liu, Shuying</dc:contributor>
    <dc:contributor>Przybylski, Michael</dc:contributor>
    <dcterms:abstract xml:lang="eng">In order to gain a comprehensive insight into the complexes of human ribosomal protein L7 with protein G in a certain degree, an investigation on the complexes of five synthetic L7 peptides, containing the basic-region-leucine-zipper (BZIP)-like domain (aa 15–49), with protein G was performed using nanoelectrospray ionization mass spectrometry (nanoESI-MS). Circular dichroism (CD) was used to characterize the secondary structures of L7 peptides. The characteristics of the complexes between L7 peptides and protein G were studied under various conditions, such as molar ratio of ligands, solvent condition, declustering potential, and peptide sequence. The stability of the complexes is found to decrease with increased declustering potential (&gt;20 V), decreased pH (&lt;5), increased pH (&gt;5), while L7 peptide sequence had no obvious effect on the complex formation. Taken together, the complexes of L7 peptides with protein G are specific noncovalent binding with 1:1 stoichiometry. Because of the availability of synthetic L7 peptides, they might be used as baits to discover the binding partners of protein L7. Furthermore, the elaboration of the binding mechanisms of L7 peptides with protein G could benefit further application of protein G.</dcterms:abstract>
    <dc:creator>Ma, Li</dc:creator>
    <dc:language>eng</dc:language>
    <dc:contributor>Kohlmann, Markus</dc:contributor>
    <dc:contributor>Ma, Li</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Krawinkel, Ulrich</dc:creator>
    <dc:contributor>Wochner, Michael</dc:contributor>
    <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
Alliance license
Corresponding Authors der Uni Konstanz vorhanden
International Co-Authors
Bibliography of Konstanz
Yes
Refereed