Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 66, Issue 3, Pages 159-162Publisher
SPRINGER
DOI: 10.1007/s10858-016-0069-2
Keywords
Amyloid fibrils; Intrinsically disordered domains; Resonance assignment; Solid-state NMR
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Funding
- University of Southern California
- Whitehall Foundation
- National Institutes of Health: NIGMS [R01GM110521]
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Several amyloid fibrils have cores framed by highly dynamic, intrinsically disordered, domains that can play important roles for function and toxicity. To study these domains in detail using solid-state NMR spectroscopy, site-specific resonance assignments are required. Although the rapid dynamics of these domains lead to considerable averaging of orientation-dependent NMR interactions and thereby line-narrowing, the proton linewidths observed in these samples is far larger than what is regularly observed in solution. Here, we show that it is nevertheless possible to record 3D HNCO, HNCA, and HNcoCA spectra on these intrinsically disordered domains and to obtain site-specific assignments.
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