Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils.

Huynen, Céline; Willet, Nicolas; Buell, Alexander K; Duwez, Anne-Sophie; Jerôme, Christine; Dumoulin, Mireille

Huynen, Céline; Willet, Nicolas; Buell, Alexander K; Duwez, Anne-Sophie; Jerôme, Christine; Dumoulin, Mireille.

Afiliação

Huynen C; Laboratory of Enzymology and Protein Folding, Centre for Protein Engineering, University of Liege, Liege, Belgium.
Willet N; Nanochemistry and Molecular Systems, Department of Chemistry, University of Liege, Liege, Belgium.
Buell AK; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Duwez AS; Nanochemistry and Molecular Systems, Department of Chemistry, University of Liege, Liege, Belgium.
Jerôme C; Center for Education and Research on Macromolecules (CERM), Department of Chemistry, University of Liege, Liege, Belgium.
Dumoulin M; Laboratory of Enzymology and Protein Folding, Centre for Protein Engineering, University of Liege, Liege, Belgium. Electronic address: mdumoulin@ulg.ac.be.

Biochim Biophys Acta ; 1854(3): 239-48, 2015 Mar.

Article em En | MEDLINE | ID: mdl-25489872

Assuntos

Amiloide/química; Amiloide/ultraestrutura; Peptídeos/química; Sítios de Ligação; Complexos Multiproteicos/química; Complexos Multiproteicos/ultraestrutura; Ligação Proteica; Conformação Proteica

Palavras-chave

Amyloid fibrils; Atomic force microscopy (AFM); BlaP-polyQ chimeras; Fibril elongation; Fibril nucleation; Quartz crystal microbalance (QCM)

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Amiloide Idioma: En Revista: Biochim Biophys Acta Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Bélgica País de publicação: Holanda

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