ArticleJournal of biomolecular NMR2011
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- Probing rare and short-lived conformational states in nucleic acids using off-resonance carbonyl and guanidino carbon RJournal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Megahertz pulse trains enable multi-hit serial femtosecond crystallography experiments at X-ray free electron lasers.Nature communications · 2022Article
- Functional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation.Science advances · 2019Article
- Experimental pKChembiochem : a European journal of chemical biology · 2019Article
- Conformational exchange of aromatic side chains byJournal of biomolecular NMR · 2018Article
- Site-selectiveJournal of biomolecular NMR · 2017Article
- A Unique and Simple Approach to Improve Sensitivity inMolecules (Basel, Switzerland) · 2017Article
- Site-selectiveJournal of biomolecular NMR · 2017Article
- Physicochemical Properties of Ion Pairs of Biological Macromolecules.Biomolecules · 2015Review
- Dynamic Equilibria of Short-Range Electrostatic Interactions at Molecular Interfaces of Protein-DNA Complexes.The journal of physical chemistry letters · 2015Article
- Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection.Journal of biomolecular NMR · 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
- Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonuclease H.Journal of the American Chemical Society · 2013Article
- Protein conformational exchange measured by 1H R1ρ relaxation dispersion of methyl groups.Journal of biomolecular NMR · 2013Article
- Probing slowly exchanging protein systems via ¹³Cα-CEST: monitoring folding of the Im7 protein.Journal of biomolecular NMR · 2013Article
- Specific 12CβD(2)12CγD(2)S13CεHD(2) isotopomer labeling of methionine to characterize protein dynamics by 1H and 13C NMR relaxation dispersion.Journal of the American Chemical Society · 2012Article
- Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected ¹³C CPMG relaxation dispersion.Journal of biomolecular NMR · 2012Article
- Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1ρ): an application to αB-crystallin.Journal of biomolecular NMR · 2012Article
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2 authors at 1 institution in 1 country.
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Abstract
A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly (13)C labeled proteins. The methodology has been tested using the 87-residue colicin E7 immunity protein, Im7, which is known to fold via a partially structured low populated intermediate that interconverts with the folded, ground state on the millisecond time-scale. Comparison of exchange parameters extracted for this folding 'reaction' using the present methodology with those obtained from more 'traditional' (15)N and backbone carbonyl probes establishes the utility of the approach. The extracted excited state side-chain carbonyl chemical shifts indicate that the Asx/Glx side-chains are predominantly unstructured in the Im7 folding intermediate. However, several crucial salt-bridges that exist in the native structure appear to be already formed in the excited state, either in part or in full. This information, in concert with that obtained from existing backbone and side-chain methyl relaxation dispersion experiments, will ultimately facilitate a detailed description of the structure of the Im7 folding intermediate.
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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.