ArticleMagnetic resonance (Gottingen, Germany)2020
Paramagpy: software for fitting magnetic susceptibility tensors using paramagnetic effects measured in NMR spectra.
Article in Magnetic resonance (Gottingen, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
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- αStructure (London, England : 1993) · 2024Article
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- Unexpected dynamics in femtomolar complexes of binding proteins with peptides.Nature communications · 2023Article
- Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction.Journal of biomolecular NMR · 2023Article
- Ligand-Capped Cobalt(II) Multiplies the Value of the Double-Histidine Motif for PCS NMR Studies.Journal of the American Chemical Society · 2023Article
- The Q163C/Q309C mutant of αMI-domain is an active variant suitable for NMR characterization.PloS one · 2023Article
- Reweighting methods for elucidation of conformation ensembles of proteins.Current opinion in structural biology · 2022Review
- NMR analysis suggests the terminal domains of Robo1 remain extended but are rigidified in the presence of heparan sulfate.Scientific reports · 2022Article
- Incorporation of residual chemical shift anisotropy into the treatment ofJournal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins.Journal of biomolecular NMR · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Assignment of Ala, Ile, LeuBiomolecular NMR assignments · 2022Article
- Article
- Characterizing conformational ensembles of multi-domain proteins using anisotropic paramagnetic NMR restraints.Biophysical reviews · 2022Review
- Site-selective generation of lanthanoid binding sites on proteins using 4-fluoro-2,6-dicyanopyridine.Magnetic resonance (Gottingen, Germany) · 2022Article
- Localising individual atoms of tryptophan side chains in the metallo-Magnetic resonance (Gottingen, Germany) · 2022Article
- Localising nuclear spins by pseudocontact shifts from a single tagging site.Magnetic resonance (Gottingen, Germany) · 2022Article
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Authors and funding
3 authors.
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Abstract
Paramagnetic metal ions with fast-relaxing electrons generate pseudocontact shifts (PCSs), residual dipolar couplings (RDCs), paramagnetic relaxation enhancements (PREs) and cross-correlated relaxation (CCR) in the nuclear magnetic resonance (NMR) spectra of the molecules they bind to. These effects offer long-range structural information in molecules equipped with binding sites for such metal ions. Here we present the new open-source software Paramagpy, which has been written in Python 3 with a graphic user interface. Paramagpy combines the functionalities of different currently available programs to support the fitting of magnetic susceptibility tensors using PCS, RDC, PRE and CCR data and molecular coordinates in Protein Data Bank (PDB) format, including a convenient graphical user interface. Paramagpy uses efficient fitting algorithms to avoid local minima and supports corrections to back-calculated PCS and PRE data arising from cross-correlation effects with chemical shift tensors. The source code is available from 10.5281/zenodo.3594568 .
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