ArticleNature protocols2009
Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy.
Article in Nature protocols, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Synthesis of SelectivelyChemistry (Weinheim an der Bergstrasse, Germany) · 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
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- Post-translational insertion of boron in proteins to probe and modulate function.Nature chemical biology · 2021Article
- A CEST NMR experiment to obtain glycineJournal of biomolecular NMR · 2020Article
- Structure Determination by Single-Particle Cryo-Electron Microscopy: Only the Sky (and Intrinsic Disorder) is the Limit.International journal of molecular sciences · 2019Review
- Late metabolic precursors for selective aromatic residue labeling.Journal of biomolecular NMR · 2018Review
- Applications of NMR and computational methodologies to study protein dynamics.Archives of biochemistry and biophysics · 2017Review
- Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer.Journal of biomolecular NMR · 2017Review
- Atomistic picture of conformational exchange in a T4 lysozyme cavity mutant: an experiment-guided molecular dynamics study.Chemical science · 2016Article
- The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats.Nucleic acids research · 2016Article
- Functional advantages of dynamic protein disorder.FEBS letters · 2015Review
- Fractional enrichment of proteins using [2-(13)C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity.Journal of biomolecular NMR · 2015Article
- Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.Protein science : a publication of the Protein Society · 2015Article
- The dynamic duo: combining NMR and small angle scattering in structural biology.Protein science : a publication of the Protein Society · 2014Review
- Revealing the properties of plant defensins through dynamics.Molecules (Basel, Switzerland) · 2013Review
- Article
- An introduction to NMR-based approaches for measuring protein dynamics.Biochimica et biophysica acta · 2011Review
- Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r).Journal of the American Chemical Society · 2010Article
- Protein flexibility and conformational entropy in ligand design targeting the carbohydrate recognition domain of galectin-3.Journal of the American Chemical Society · 2010Article
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4 authors.
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Abstract
The utility of nuclear magnetic resonance (NMR) spectroscopy as a tool for the study of biomolecular structure and dynamics has benefited from the development of facile labeling methods that incorporate NMR active probes at key positions in the molecule. Here we describe a protocol for the labeling of proteins that facilitates their study using a technique that is sensitive to millisecond conformational exchange processes. The samples necessary for an analysis of exchange dynamics are discussed, using the Abp1p SH3 domain from Saccharomyces cerevisiae as an example. For this system, the time frame for production of each sample, including in vitro refolding, is about 80 h. The samples so produced facilitate the measurement of accurate chemical shifts of low populated, invisible conformers that are part of the exchange pathway. The accuracy of the methodology has been established experimentally and the chemical shifts that are obtained provide important restraints in structure calculations of the excited state.
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