ArticlePLoS computational biology2022
Linear discriminant analysis reveals hidden patterns in NMR chemical shifts of intrinsically disordered proteins.
Article in PLoS computational biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 6 citations in OpenAlex.
- Harmonizing Peak Matching between Multidimensional NMR Spectra.Journal of chemical information and modeling · 2026Article
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- AI-driven differentiation of 2D proximal femur morphometry and hounsfield units for integrated forensic estimation of sex, stature, and age in a modern Thai dry bone sample.Anatomical science international · 2026Article
- WNetAlign: fast and accurate spectra alignment using truncated Wasserstein distance and network simplex.Briefings in bioinformatics · 2026Article
- Natural Fatty Acids as Dual ACE2-Inflammatory Modulators: Integrated Computational Framework for Pandemic Preparedness.International journal of molecular sciences · 2025Article
- Using temperature coefficients to support resonance assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2025Article
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5 authors at 2 institutions in 1 country.
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Abstract
NMR spectroscopy is key in the study of intrinsically disordered proteins (IDPs). Yet, even the first step in such an analysis-the assignment of observed resonances to particular nuclei-is often problematic due to low peak dispersion in the spectra of IDPs. We show that the assignment process can be aided by finding "hidden" chemical shift patterns specific to the amino acid residue types. We find such patterns in the training data from the Biological Magnetic Resonance Bank using linear discriminant analysis, and then use them to classify spin systems in an α-synuclein sample prepared by us. We describe two situations in which the procedure can greatly facilitate the analysis of NMR spectra. The first involves the mapping of spin systems chains onto the protein sequence, which is part of the assignment procedure-a prerequisite for any NMR-based protein analysis. In the second, the method supports assignment transfer between similar samples. We conducted experiments to demonstrate these cases, and both times the majority of spin systems could be unambiguously assigned to the correct residue types.
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