ArticleProceedings of the National Academy of Sciences of the United States of America2014
Measuring hydrogen exchange rates in invisible protein excited states.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Substrate specificity in a designed RAS-targeting protease is coupled to active site and distal motions.bioRxiv : the preprint server for biology · 2026Article
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- Indirect Detection of the Protons in and around Biradicals and their Mechanistic Role in MAS-DNP.The journal of physical chemistry letters · 2025Article
- Measuring Hydroxyl Exchange Rates in Glycans Using a Synergistic Combination of Saturation Transfer and Relaxation Dispersion NMR.Journal of the American Chemical Society · 2024Article
- Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions.Molecular biology and evolution · 2022Article
- Toward a proper interpretation of hydrogen exchange data in disordered proteins.Biophysical journal · 2021Article
- Integrated Computational Approaches and Tools forAllosteric Drug Discovery.International journal of molecular sciences · 2020Review
- Allosteric Regulation at the Crossroads of New Technologies: Multiscale Modeling, Networks, and Machine Learning.Frontiers in molecular biosciences · 2020Review
- Exchangeable deuterons introduce artifacts in amideJournal of biomolecular NMR · 2019Article
- Atomic structures of excited state A-T Hoogsteen base pairs in duplex DNA by combining NMR relaxation dispersion, mutagenesis, and chemical shift calculations.Journal of biomolecular NMR · 2018Article
- Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer.Journal of biomolecular NMR · 2017Review
- Hsp70 biases the folding pathways of client proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Chemo-enzymatic synthesis of site-specific isotopically labeled nucleotides for use in NMR resonance assignment, dynamics and structural characterizations.Nucleic acids research · 2016Article
- Measuring Residual Dipolar Couplings in Excited Conformational States of Nucleic Acids by CEST NMR Spectroscopy.Journal of the American Chemical Society · 2015Article
- Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- pH-dependent transient conformational states control optical properties in cyan fluorescent protein.Journal of the American Chemical Society · 2015Article
- Visualizing transient dark states by NMR spectroscopy.Quarterly reviews of biophysics · 2015Article
- Predicting protein backbone chemical shifts from Cα coordinates: extracting high resolution experimental observables from low resolution models.Journal of chemical theory and computation · 2015Article
- Characterizing RNA Excited States Using NMR Relaxation Dispersion.Methods in enzymology · 2015Article
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3 authors.
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Abstract
Hydrogen exchange rates have become a valuable probe for studying the relationship between dynamics and structure and for dissecting the mechanism by which proteins fold to their native conformation. Typically measured rates correspond to averages over all protein states from which hydrogen exchange can occur. Here we describe a new NMR experiment based on chemical exchange saturation transfer that provides an avenue for obtaining uncontaminated, per-residue amide hydrogen exchange rates for interconverting native and invisible states so long as they can be separated on the basis of distinct (15)N chemical shifts. The approach is applied to the folding reaction of the Fyn SH3 domain that exchanges between a highly populated, NMR-visible native state and a conformationally excited, NMR-invisible state, corresponding to the unfolded ensemble. Excellent agreement between experimentally derived hydrogen exchange rates of the excited state at a pair of pHs is obtained, taking into account the expected dependence of exchange on pH. Extracted rates for the unfolded ensemble have been used to test hydrogen exchange predictions based on the primary protein sequence that are used in many analyses of solvent exchange rates, with a Pearson correlation coefficient of 0.84 obtained.
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