期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 132, 期 39, 页码 13765-13775出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja104213J
关键词
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资金
- Swiss National Science Foundation
- TH-system of the ETH Zurich
- European Union
We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal priori HET-s in its amyloid form. On the basis of 134 unambiguous distance restraints, we recently showed that HETs-(218-289) in its fibrillar state forms a left-handed beta-solenoid, and an atomic-resolution NMR structure of the triangular core was determined from unambiguous restraints only. In this paper, we go considerably further and present a comprehensive protocol using six differently labeled samples, a collection of optimized solid-state NMR experiments, and adapted structure calculation protocols. The high-resolution structure obtained includes the less ordered but biologically important C-terminal part and improves the overall accuracy by including a large number of ambiguous distance restraints.
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