ArticleJournal of biomolecular NMR2013
Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
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 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed.
- Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes.Nature chemistry · 2026Article
- Conformation-selective detection of residues in solid proteins under magic-angle-spinning.Journal of biomolecular NMR · 2026Article
- Proton-Detected Solid-State NMR for Deciphering Structural Polymorphism and Dynamic Heterogeneity of Cellular Carbohydrates in Pathogenic Fungi.Journal of the American Chemical Society · 2025Article
- Probing the Dynamics of Yersinia Adhesin A (YadA) in Outer Membranes Hints at Requirements for β-Barrel Membrane Insertion.Journal of the American Chemical Society · 2025Article
- Conformational Dynamics of BacteriochlorophyllThe journal of physical chemistry. B · 2025Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR.Magnetic resonance (Gottingen, Germany) · 2024Article
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Accurate Determination of Motional Amplitudes in Biomolecules by Solid-State NMR.ACS physical chemistry Au · 2023Article
- Review
- Direct investigation of the reorientational dynamics of A-site cations in 2D organic-inorganic hybrid perovskite by solid-state NMR.Nature communications · 2022Article
- Transferred-Rotational-Echo Double Resonance.The journal of physical chemistry. A · 2021Article
- Model-Free or Not?Frontiers in molecular biosciences · 2021Review
- Conformational Stability and Dynamics in Crystals Recapitulate Protein Behavior in Solution.Biophysical journal · 2020Article
- Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.Biochimica et biophysica acta. Biomembranes · 2020Article
- ssNMRlib: a comprehensive library and tool box for acquisition of solid-state nuclear magnetic resonance experiments on Bruker spectrometers.Magnetic resonance (Gottingen, Germany) · 2020Article
- Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using ComplementaryJournal of the American Chemical Society · 2019Article
- Dynamics of the Proline-Rich C-Terminus of Huntingtin Exon-1 Fibrils.The journal of physical chemistry. B · 2018Article
- Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.Methods (San Diego, Calif.) · 2018Review
- Microsecond motions probed by near-rotary-resonance RJournal of biomolecular NMR · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Solid-state NMR provides insight into protein motion over time scales ranging from picoseconds to seconds. While in solution state the methodology to measure protein dynamics is well established, there is currently no such consensus protocol for measuring dynamics in solids. In this article, we perform a detailed investigation of measurement protocols for fast motions, i.e. motions ranging from picoseconds to a few microseconds, which is the range covered by dipolar coupling and relaxation experiments. We perform a detailed theoretical investigation how dipolar couplings and relaxation data can provide information about amplitudes and time scales of local motion. We show that the measurement of dipolar couplings is crucial for obtaining accurate motional parameters, while systematic errors are found when only relaxation data are used. Based on this realization, we investigate how the REDOR experiment can provide such data in a very accurate manner. We identify that with accurate rf calibration, and explicit consideration of rf field inhomogeneities, one can obtain highly accurate absolute order parameters. We then perform joint model-free analyses of 6 relaxation data sets and dipolar couplings, based on previously existing, as well as new data sets on microcrystalline ubiquitin. We show that nanosecond motion can be detected primarily in loop regions, and compare solid-state data to solution-state relaxation and RDC analyses. The protocols investigated here will serve as a useful basis towards the establishment of a routine protocol for the characterization of ps-μs motions in proteins by solid-state NMR.
Indexed as
Identifiers
What OpenQuestion holds
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.