Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
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SHR Neuro Krebs Kardio Lipid Stoffw Microb
Pritišanac, I; Würz, JM; Alderson, TR; Güntert, P.
Automatic structure-based NMR methyl resonance assignment in large proteins.
Nat Commun. 2019; 10(1):4922
Doi: 10.1038/s41467-019-12837-8
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- Führende Autor*innen der Med Uni Graz
- Pritisanac Iva
- Co-Autor*innen der Med Uni Graz
- Alderson Thomas Reid
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- Abstract:
- Isotopically labeled methyl groups provide NMR probes in large, otherwise deuterated proteins. However, the resonance assignment constitutes a bottleneck for broader applicability of methyl-based NMR. Here, we present the automated MethylFLYA method for the assignment of methyl groups that is based on methyl-methyl nuclear Overhauser effect spectroscopy (NOESY) peak lists. MethylFLYA is applied to five proteins (28-358 kDa) comprising a total of 708 isotope-labeled methyl groups, of which 612 contribute NOESY cross peaks. MethylFLYA confidently assigns 488 methyl groups, i.e. 80% of those with NOESY data. Of these, 459 agree with the reference, 6 were different, and 23 were without reference assignment. MethylFLYA assigns significantly more methyl groups than alternative algorithms, has an average error rate of 1%, modest runtimes of 0.4-1.2 h, and can handle arbitrary isotope labeling patterns and data from other types of NMR spectra.
- Find related publications in this database (using NLM MeSH Indexing)
- Algorithms - administration & dosage
- Automation - methods
- Methylation - administration & dosage
- Models, Molecular - administration & dosage
- Molecular Weight - administration & dosage
- Nuclear Magnetic Resonance, Biomolecular - methods
- Proteins - chemistry
- Software - administration & dosage