Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR.

ABSTRACT: Several human diseases are associated with the formation of amyloid aggregates, but experimental characterization of these amyloid fibrils and their oligomeric precursors has remained challenging. Experimental and computational analysis of simpler model systems has therefore been necessary, for instance, on the peptide fragment GNNQQNY7−13 of yeast prion protein Sup35p. Expanding on a previous publication, we report here a detailed structural characterization of GNNQQNY fibrils using magic angle spinning (MAS) NMR. On the basis of additional chemical shift assignments we confirm the coexistence of three distinct peptide conformations within the fibrillar samples, as reflected in substantial chemical shift differences. Backbone torsion angle measurements indicate that the basic structure of

SUBMITTER: van der Wel PC 

PROVIDER: S-EPMC3026921 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature