Publikation:

Detecting Relationships between Amino Acid Residue Sequences and 3D Protein Structures based on a New Class of Rotamer Libraries

Lade...
Vorschaubild

Dateien

gcb98_prot.pdf
gcb98_prot.pdfGröße: 1.1 MBDownloads: 60

Datum

1998

Autor:innen

Hinneburg, Alexander
Brandt, Wolfgang

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

DOI (zitierfähiger Link)
ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Beitrag zu einem Konferenzband
Publikationsstatus
Published

Erschienen in

Proceedings of the German Conference on Bioinformatics (GCB'98), Köln, September, 1998. 1998

Zusammenfassung

In the past a good number of rotamer libraries have been published, which allow a deeper understanding of the conformational behaviour of amino acid residues in proteins. Since the number of available high resolution X-ray protein structures has grown significantly over the last years, a more comprehensive analysis of the conformational behaviour is possible today. In this paper, we present a method to compile a new class of rotamer libraries for detecting interesting relationships between residue conformations and their sequential context in proteins. The method is based on a new algorithm for clustering residue conformations. To demonstrate the effectivity of our method we apply our algorithm to a library consisting of all 8000 tripetid fragments formed by the 20 native amino acids. The analysis shows some very interesting new results, namely that some specific tripeptid fragments show some unexpected conformation of residues instead of the highly preferred conformation. In the neighborhood of two asparagin residues, for example, threonin avoids the conformation which is most likely to occur otherwise. The new insights obtained by the analysis are important in understanding the formation and prevention of secondary structure elements and will consequently be crucial for improving the state-of-the-art of protein folding.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
004 Informatik

Schlagwörter

rotamer library, cluster algorithm, conformational analysis, tripeptids, protein folding

Konferenz

GCB, Sept. 1998, Köln
Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690HINNEBURG, Alexander, Daniel A. KEIM, Wolfgang BRANDT, 1998. Detecting Relationships between Amino Acid Residue Sequences and 3D Protein Structures based on a New Class of Rotamer Libraries. GCB. Köln, Sept. 1998. In: Proceedings of the German Conference on Bioinformatics (GCB'98), Köln, September, 1998. 1998
BibTex
@inproceedings{Hinneburg1998Detec-5855,
  year={1998},
  title={Detecting Relationships between Amino Acid Residue Sequences and 3D Protein Structures based on a New Class of Rotamer Libraries},
  booktitle={Proceedings of the German Conference on Bioinformatics (GCB'98), Köln, September, 1998},
  author={Hinneburg, Alexander and Keim, Daniel A. and Brandt, Wolfgang}
}
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/123456789/5855">
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:contributor>Keim, Daniel A.</dc:contributor>
    <dc:language>eng</dc:language>
    <dcterms:title>Detecting Relationships between Amino Acid Residue Sequences and 3D Protein Structures based on a New Class of Rotamer Libraries</dcterms:title>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/36"/>
    <dc:format>application/pdf</dc:format>
    <dcterms:abstract xml:lang="eng">In the past a good number of rotamer libraries have been published, which allow a deeper understanding of the conformational behaviour of amino acid residues in proteins. Since the number of available high resolution X-ray protein structures has grown significantly over the last years, a more comprehensive analysis of the conformational behaviour is possible today. In this paper, we present a method to compile a new class of rotamer libraries for detecting interesting relationships between residue conformations and their sequential context in proteins. The method is based on a new algorithm for clustering residue conformations. To demonstrate the effectivity of our method we apply our algorithm to a library consisting of all 8000 tripetid fragments formed by the 20 native amino acids. The analysis shows some very interesting new results, namely that some specific tripeptid fragments show some unexpected conformation of residues instead of the highly preferred conformation. In the neighborhood of two asparagin residues, for example, threonin avoids the conformation which is most likely to occur otherwise. The new insights obtained by the analysis are important in understanding the formation and prevention of secondary structure elements and will consequently be crucial for improving the state-of-the-art of protein folding.</dcterms:abstract>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T16:00:42Z</dc:date>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:contributor>Hinneburg, Alexander</dc:contributor>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/5855/1/gcb98_prot.pdf"/>
    <dc:creator>Brandt, Wolfgang</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/36"/>
    <dcterms:bibliographicCitation>First publ. in: Proceedings / German Conference on Bioinformatics (GCB'98), Köln, September, 1998</dcterms:bibliographicCitation>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dc:contributor>Brandt, Wolfgang</dc:contributor>
    <dc:creator>Hinneburg, Alexander</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T16:00:42Z</dcterms:available>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/5855"/>
    <dcterms:issued>1998</dcterms:issued>
    <dc:creator>Keim, Daniel A.</dc:creator>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/5855/1/gcb98_prot.pdf"/>
  </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
Diese Publikation teilen