ArticleJournal of biomolecular NMR2013
Probing slowly exchanging protein systems via ¹³Cα-CEST: monitoring folding of the Im7 protein.
Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- A CEST NMR experiment to obtain glycineJournal of biomolecular NMR · 2020Article
- Exchangeable deuterons introduce artifacts in amideJournal of biomolecular NMR · 2019Article
- Equilibrium folding dynamics of meACP in water, heavy water, and low concentration of urea.Scientific reports · 2017Article
- Probing the excited-state chemical shifts and exchange parameters by nitrogen-decoupled amide proton chemical exchange saturation transfer (HNChemical communications (Cambridge, England) · 2017Article
- Chemo-enzymatic synthesis of site-specific isotopically labeled nucleotides for use in NMR resonance assignment, dynamics and structural characterizations.Nucleic acids research · 2016Article
- Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.Angewandte Chemie (International ed. in English) · 2016Article
- 13Cα CEST experiment on uniformly 13C-labeled proteins.Journal of biomolecular NMR · 2015Article
- Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using ¹³C(methyl)-DEST and lifetime line broadening.Angewandte Chemie (International ed. in English) · 2014Article
- Measurement of histidine pKa values and tautomer populations in invisible protein states.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Chemical exchange in biomacromolecules: past, present, and future.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Characterizing slow chemical exchange in nucleic acids by carbon CEST and low spin-lock field R(1ρ) NMR spectroscopy.Journal of the American Chemical Society · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A¹³C(α) chemical exchange saturation transfer based experiment is presented for the study of protein systems undergoing slow interconversion between an 'observable' ground state and one or more 'invisible' excited states. Here a labeling strategy whereby [2-(13)C]-glucose is the sole carbon source is exploited, producing proteins with ¹³C at the C(α) position, while the majority of residues remain unlabeled at CO or C(β). The new experiment is demonstrated with an application to the folding reaction of the Im7 protein that involves an on-pathway excited state. The obtained excited state (13)C(α) chemical shifts are cross validated by comparison to values extracted from analysis of CPMG relaxation dispersion profiles, establishing the utility of the methodology.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.