ArticleJournal of biomolecular NMR2019
Exchange saturation transfer and associated NMR techniques for studies of protein interactions involving high-molecular-weight systems.
Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Going high-throughput: Dynamic conformations and interactionsMagnetic resonance letters · 2027Review
- Two-dimensional NMR from a single pulse: Reconstructing heteronuclear 2D spectra via off-resonance decoupling and deep neural networks.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Elucidating Surface Adsorption of Lithium Ions on Electrode Materials UsingJournal of the American Chemical Society · 2025Article
- Mapping the FF domain folding pathway via structures of transiently populated folding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Decoding chaperone complexes: Insights from NMR spectroscopy.Biophysics reviews · 2024Review
- NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity.Nature communications · 2024Article
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- NMR spectroscopy, excited states and relevance to problems in cell biology - transient pre-nucleation tetramerization of huntingtin and insights into Huntington's disease.Journal of cell science · 2022Article
- Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.Annual review of biophysics · 2022Review
- NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- 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
- Quantitative NMR Study of Insulin-Degrading Enzyme Using Amyloid-β and HIV-1 p6 Elucidates Its Chaperone Activity.Biochemistry · 2021Article
- Probing the Interaction of Huntingtin Exon-1 Polypeptides with the Chaperonin Nanomachine GroEL.Chembiochem : a European journal of chemical biology · 2021Article
- A CEST NMR experiment to obtain glycineJournal of biomolecular NMR · 2020Article
- Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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2 authors.
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Abstract
A brief overview of theoretical and experimental aspects of the Dark state Exchange Saturation Transfer (DEST) and lifetime line broadening ([Formula: see text]) NMR methodologies is presented from a physico-chemical perspective. We describe how the field-dependence of [Formula: see text] can be used for determining the exchange regime on the transverse spin relaxation time-scale. Some limitations of DEST/[Formula: see text] methodology in applications to molecular systems with intermediate molecular weights are discussed, and the means of overcoming these limitations via the use of closely related exchange NMR techniques is presented. Finally, several applications of DEST/[Formula: see text] methodology are described from a methodological viewpoint, with an emphasis on providing examples of how kinetic and relaxation parameters of exchange can be reliably extracted from the experimental data in each particular case.
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