期刊
JOURNAL OF BIOMOLECULAR NMR
卷 56, 期 3, 页码 243-254出版社
SPRINGER
DOI: 10.1007/s10858-013-9742-x
关键词
Automated assignment; Sequence-specific assignment; Amyloid; CYANA; FLYA
资金
- Lichtenberg program of the Volkswagen Foundation
- Deutsche Forschungsgemeinschaft (DFG)
- Swiss National Science Foundation [200020_124611]
- Agence Nationale de la Recherche [SIMI8 2012]
- European Commission [Bio-NMR 261863]
- Swiss National Science Foundation (SNF) [200020_124611] Funding Source: Swiss National Science Foundation (SNF)
Solid-state NMR is an emerging structure determination technique for crystalline and non-crystalline protein assemblies, e.g., amyloids. Resonance assignment constitutes the first and often very time-consuming step to a structure. We present ssFLYA, a generally applicable algorithm for automatic assignment of protein solid-state NMR spectra. Application to microcrystals of ubiquitin and the Ure2 prion C-terminal domain, as well as amyloids of HET-s(218-289) and alpha-synuclein yielded 88-97 % correctness for the backbone and side-chain assignments that are classified as self-consistent by the algorithm, and 77-90 % correctness if also assignments classified as tentative by the algorithm are included.
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