ArticleThe journal of physical chemistry letters2020
Multiquantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.
Article in The journal of physical chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- Arginine: I. Interactions of Its Guanidinium Moiety with Branched Aliphatic Side Chains.The journal of physical chemistry. B · 2025Article
- Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation.Journal of the American Chemical Society · 2024Article
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- Slow Rotational Dynamics of Cytosine NHBiochemistry · 2022Article
- Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy.Journal of magnetic resonance open · 2022Article
- Hindered Rotations of Protein Asparagine/Glutamine Side-Chain NHThe journal of physical chemistry letters · 2021Article
- The A39G FF domain folds on a volcano-shaped free energy surface via separate pathways.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Combined High-Pressure and Multiquantum NMR and Molecular Simulation Propose a Role for N-Terminal Salt Bridges in Amyloid-Beta.The journal of physical chemistry letters · 2021Article
- Measuring radiofrequency fields in NMR spectroscopy using offset-dependent nutation profiles.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2021Article
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3 authors.
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Abstract
Chemical exchange saturation transfer (CEST) NMR experiments have emerged as a powerful tool for characterizing dynamics in proteins. We show here that the CEST approach can be extended to systems with symmetrical exchange, where the NMR signals of all exchanging species are severely broadened. To achieve this, multiquantum CEST (MQ-CEST) is introduced, where the CEST pulse is applied to a longitudinal multispin order density element and the CEST profiles are encoded onto nonbroadened nuclei. The MQ-CEST approach is demonstrated on the restricted rotation of guanidinium groups in arginine residues within proteins. These groups and their dynamics are essential for many enzymes and for noncovalent interactions through the formation of hydrogen bonds, salt-bridges, and π-stacking interactions, and their rate of rotation is highly indicative of the extent of interactions formed. The MQ-CEST method is successfully applied to guanidinium groups in the 19 kDa L99A mutant of T4 lysozyme.
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