[NMR paper] Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins
Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins
NMR spectroscopy allows the study of biomolecules in close-to-native conditions. Structural information can be inferred from the NMR spectra when an assignment is available. Protein assignment is usually a time-consuming task, being specially challenging in the case of large, supramolecular systems. Here, we present an extension of existing state-of-the-art strategies for methyl group assignment that partially overcomes signal overlapping and other...
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04-11-2022 10:19 AM
Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins
Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins
Abstract
NMR spectroscopy allows the study of biomolecules in close-to-native conditions. Structural information can be inferred from the NMR spectra when an assignment is available. Protein assignment is usually a time-consuming task, being specially challenging in the case of large, supramolecular systems. Here, we present an extension of existing state-of-the-art strategies for methyl group assignment that...
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04-10-2022 09:31 PM
[NMR paper] Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Related Articles Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Nat Commun. 2021 Jan 29;12(1):691
Authors: Nerli S, De Paula VS, McShan AC, Sgourakis NG
Abstract
Methyl-specific isotope labeling is a powerful tool to study the structure, dynamics and interactions of large proteins and protein complexes by solution-state NMR. However, widespread applications of this methodology have been limited by challenges in...
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01-31-2021 02:47 PM
3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample
3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample
Abstract The feasibility of practically complete backbone and ILV methyl chemical shift assignments from a single -labeled protein sample of the truncated form of ligand-free Bst-Tyrosyl tRNA Synthetase (Bst-ﾎ?YRS), a 319-residue predominantly helical homodimer, is established. Protonation of ILV residues at methyl positions does not appreciably detract from the quality of TROSY triple resonance data. The assignments are performed at 40 ﾂｰC to improve the sensitivity of...
Backbone-independent NMR resonance assignments of methyl probes in large proteins - Nature.com
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