ArticleJournal of biomolecular NMR2012
A 2D ¹³C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
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- 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
- The conformational landscape of fold-switcher KaiB is tuned to the circadian rhythm timescale.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy.Science advances · 2022Article
- Sensitivity Enhancement by Progressive Saturation of the Proton Reservoir: A Solid-State NMR Analogue of Chemical Exchange Saturation Transfer.Journal of the American Chemical Society · 2021Article
- Opening of a cryptic pocket in β-lactamase increases penicillinase activity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A quantitative model predicts how mNature communications · 2021Article
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- Elucidating dissociation activation energies in host-guest assemblies featuring fast exchange dynamics.Chemical science · 2020Article
- A CEST NMR experiment to obtain glycineJournal of biomolecular NMR · 2020Article
- The precious fluorine on the ring: fluorine NMR for biological systems.Journal of biomolecular NMR · 2020Article
- A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A 300-fold enhancement of imino nucleic acid resonances by hyperpolarized water provides a new window for probing RNA refolding by 1D and 2D NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- NMR Chemical Exchange Measurements Reveal ThatJournal of the American Chemical Society · 2019Article
- RevisitingJournal of biomolecular NMR · 2019Article
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2 authors.
Funding
Abstract
A 2D (13)C Chemical Exchange Saturation Transfer (CEST) experiment is presented for studying slowly exchanging protein systems using methyl groups as probes. The utility of the method is first established through studies of protein L, a small protein, for which chemical exchange on the millisecond time-scale is not observed. Subsequently the approach is applied to a folding exchange reaction of a G48M mutant Fyn SH3 domain, for which only cross-peaks derived from the folded ('ground') state are present in spectra. Fits of (15)N and methyl (13)C CEST profiles of the Fyn SH3 domain establish that the exchange reaction involves an interchange between folded and unfolded conformers, although elevated methyl (13)C transverse relaxation rates for some of the residues of the unfolded ('invisible, excited') state indicate that it likely exchanges with a third conformation as well. In addition to the kinetics of the exchange reaction, methyl carbon chemical shifts of the excited state are also obtained from analysis of the (13)C CEST data.
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