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A method for probing the mutational landscape of amyloid structure

Motivation: Proteins of all kinds can self-assemble into highly ordered β-sheet aggregates known as amyloid fibrils, important both biologically and clinically. However, the specific molecular structure of a fibril can vary dramatically depending on sequence and environmental conditions, and mutatio...

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Detalles Bibliográficos
Autores principales: O'Donnell, Charles W., Waldispühl, Jérôme, Lis, Mieszko, Halfmann, Randal, Devadas, Srinivas, Lindquist, Susan, Berger, Bonnie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117379/
https://www.ncbi.nlm.nih.gov/pubmed/21685090
http://dx.doi.org/10.1093/bioinformatics/btr238