ArticleAngewandte Chemie (International ed. in English)2016
Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Gel-Based NMR Method for Observing Submicrosecond Protein Dynamics at Atomic Resolution.The journal of physical chemistry letters · 2026Article
- Detection of intramolecular protein dynamics on nanosecond-to-microsecond timescales by nanoparticle-assisted NMR spin relaxation (NASR).Nature protocols · 2026Review
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- Dynamics in natural and designed elastins and their relation to elastic fiber structure and recoil.Biophysical journal · 2021Article
- Extreme Nonuniform Sampling for Protein NMR Dynamics Studies in Minimal Time.Journal of the American Chemical Society · 2019Article
- Characterization of Internal Protein Dynamics and Conformational Entropy by NMR Relaxation.Methods in enzymology · 2019Article
- Fast evaluation of protein dynamics from deficientJournal of biomolecular NMR · 2018Article
- Article
- 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
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Functional motions of (15)N-labeled proteins can be monitored by solution NMR spin relaxation experiments over a broad range of timescales. These experiments however typically take of the order of several days to a week per protein. Recently, NMR chemical exchange saturation transfer (CEST) experiments have emerged to probe slow millisecond motions complementing R1ρ and CPMG-type experiments. CEST also simultaneously reports on site-specific R1 and R2 parameters. It is shown here how CEST-derived R1 and R2 relaxation parameters can be measured within a few hours at an accuracy comparable to traditional relaxation experiments. Using a "lean" version of the model-free approach S(2) order parameters can be determined that match those from the standard model-free approach applied to (15)N R1, R2 , and {(1)H}-(15)N NOE data. The new methodology, which is demonstrated for ubiquitin and arginine kinase (42 kDa), should serve as an effective screening tool of protein dynamics from picosecond-to-millisecond timescales.
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Registered trials
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