Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.

ABSTRACT: Protein magic angle spinning (MAS) NMR spectroscopy has generated structural models of several amyloid fibril systems, thus providing valuable information regarding the forces and interactions that confer the extraordinary stability of the amyloid architecture. Despite these advances, however, obtaining atomic resolution information describing the higher levels of structural organization within the fibrils remains a significant challenge. Here, we detail MAS NMR experiments and sample labeling schemes designed specifically to probe such higher order amyloid structure, and we have applied them to the fibrils formed by an eleven-residue segment of the amyloidogenic protein transthyretin (TTR(105-115)). These experiments have allowed us to define unambiguously not only the arrangement of the

SUBMITTER: Debelouchina GT 

PROVIDER: S-EPMC3909659 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature