KOPS - The Institutional Repository of the University of Konstanz

Observation of Oligomeric States Indicates a High Structural Flexibility Required for the Onset of Polyglutamine Fibrillization

Observation of Oligomeric States Indicates a High Structural Flexibility Required for the Onset of Polyglutamine Fibrillization

Cite This

Files in this item

Files Size Format View

There are no files associated with this item.

SIU, Ho-Wah, Karin HAUSER, 2022. Observation of Oligomeric States Indicates a High Structural Flexibility Required for the Onset of Polyglutamine Fibrillization. In: The Journal of Physical Chemistry Letters. American Chemical Society (ACS). 13(20), pp. 4543-4548. eISSN 1948-7185. Available under: doi: 10.1021/acs.jpclett.2c00203

@article{Siu2022-05-26Obser-57831, title={Observation of Oligomeric States Indicates a High Structural Flexibility Required for the Onset of Polyglutamine Fibrillization}, year={2022}, doi={10.1021/acs.jpclett.2c00203}, number={20}, volume={13}, journal={The Journal of Physical Chemistry Letters}, pages={4543--4548}, author={Siu, Ho-Wah and Hauser, Karin} }

<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/rdf/resource/123456789/57831"> <dc:creator>Hauser, Karin</dc:creator> <dcterms:issued>2022-05-26</dcterms:issued> <dcterms:title>Observation of Oligomeric States Indicates a High Structural Flexibility Required for the Onset of Polyglutamine Fibrillization</dcterms:title> <dc:contributor>Hauser, Karin</dc:contributor> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <dc:contributor>Siu, Ho-Wah</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-06-23T13:22:26Z</dcterms:available> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-06-23T13:22:26Z</dc:date> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <dc:language>eng</dc:language> <dc:creator>Siu, Ho-Wah</dc:creator> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/57831"/> <dcterms:abstract xml:lang="eng">Polyglutamine (polyQ) diseases are caused by misfolding and aggregation of expanded polyQ tracts in the affected protein. PolyQ fibrils have been studied in detail; however, less is known about oligomeric precursor states. By a combination of time-resolved temperature-jump (T-jump) infrared (IR) spectroscopy and an appropriately tailored polyQ model peptide, we succeeded in disentangling conformational dynamics in the heterogeneous ensemble of states evolving during aggregation. Individual structural elements could be differentiated by IR-specific signatures, i.e., hairpin monomers, β-structured oligomers, and disordered structure. Submillisecond dynamics were observed for early oligomeric states in contrast to the slow dynamics of fibril growth. We propose that a high structural flexibility of oligomers is required to initiate fibril formation, but not after a fibrillar structure has consolidated and the fibril just grows. Our study reveals that structural flexibility changes at different stages in the aggregation process, from fibril initiation to fibril growth.</dcterms:abstract> </rdf:Description> </rdf:RDF>

This item appears in the following Collection(s)

Search KOPS


Browse

My Account