ArticleJournal of biomolecular NMR2008
APSY-NMR with proteins: practical aspects and backbone assignment.
Article in Journal of biomolecular NMR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Complete protein assignment from sets of spectra recorded overnight.Journal of biomolecular NMR · 2019Article
- Automated projection spectroscopy in solid-state NMR.Journal of biomolecular NMR · 2018Review
- Molecular interactions connecting the function of the serine-arginine-rich protein SRSF1 to protein phosphatase 1.The Journal of biological chemistry · 2018Article
- XLSY: Extra-Large NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2018Article
- Segmental isotope labelling and solid-state NMR of a 12 × 59 kDa motor protein: identification of structural variability.Journal of biomolecular NMR · 2018Article
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- Dynamic Local Polymorphisms in the Gbx1 Homeodomain Induced by DNA Binding.Structure (London, England : 1993) · 2016Article
- Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif.Journal of molecular biology · 2016Article
- Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence Motif.Structure (London, England : 1993) · 2016Article
- Non-Uniform Sampling and J-UNIO Automation for Efficient Protein NMR Structure Determination.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- NMR structure determination of the protein NP_344798.1 as the first representative of Pfam PF06042.Journal of biomolecular NMR · 2015Article
- APSY-NMR for protein backbone assignment in high-throughput structural biology.Journal of biomolecular NMR · 2015Article
- J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.Journal of biomolecular NMR · 2015Article
- A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2014Article
- Strategy for automated NMR resonance assignment of RNA: application to 48-nucleotide K10.Journal of biomolecular NMR · 2014Article
- Practical aspects of NMR signal assignment in larger and challenging proteins.Progress in nuclear magnetic resonance spectroscopy · 2014Review
- NMR-profiles of protein solutions.Biopolymers · 2013Article
- Structural representative of the protein family PF14466 has a new fold and establishes links with the C2 and PLAT domains from the widely distant Pfams PF00168 and PF01477.Protein science : a publication of the Protein Society · 2013Article
- 4D experiments measured with APSY for automated backbone resonance assignments of large proteins.Journal of biomolecular NMR · 2013Article
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3 authors.
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Abstract
Automated projection spectroscopy (APSY) is an NMR technique for the recording of discrete sets of projection spectra from higher-dimensional NMR experiments, with automatic identification of the multidimensional chemical shift correlations by the dedicated algorithm GAPRO. This paper presents technical details for optimizing the set-up and the analysis of APSY-NMR experiments with proteins. Since experience so far indicates that the sensitivity for signal detection may become the principal limiting factor for applications with larger proteins or more dilute samples, we performed an APSY-NMR experiment at the limit of sensitivity, and then investigated the effects of varying selected experimental parameters. To obtain the desired reference data, a 4D APSY-HNCOCA experiment with a 12-kDa protein was recorded in 13 min. Based on the analysis of this data set and on general considerations, expressions for the sensitivity of APSY-NMR experiments have been generated to guide the selection of the projection angles, the calculation of the sweep widths, and the choice of other acquisition and processing parameters. In addition, a new peak picking routine and a new validation tool for the final result of the GAPRO spectral analysis are introduced. In continuation of previous reports on the use of APSY-NMR for sequence-specific resonance assignment of proteins, we present the results of a systematic search for suitable combinations of a minimal number of four- and five-dimensional APSY-NMR experiments that can provide the input for algorithms that generate automated protein backbone assignments.
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