ArticleJournal of biomolecular NMR2011
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
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 42 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
42 citing papers in PubMed.
- NMR spectral simplification with imidazolium ionic liquid-coated silica nanoparticles.Magnetic resonance letters · 2026Article
- Quantifying the liquid-liquid transition in cold water/glycerol mixtures by intermolecular hyperfine relaxation-induced dipolar modulation enhancement (ih-RIDME).Physical chemistry chemical physics : PCCP · 2025Article
- Solid-state NMR of membrane peptides and proteins in the lipid cubic phase.Biophysical journal · 2025Article
- Sorbitol-Based Glass Matrices Enable Dynamic Nuclear Polarization beyond 200 K.The journal of physical chemistry letters · 2024Article
- Resolution in cryogenic solid state NMR: Challenges and solutions.Protein science : a publication of the Protein Society · 2024Review
- A high-field cellular DNP-supported solid-state NMR approach to study proteins with sub-cellular specificity.Chemical science · 2023Article
- Stability and expression of SARS-CoV-2 spike-protein mutations.Molecular and cellular biochemistry · 2023Article
- Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR.Journal of biomolecular NMR · 2022Article
- DNP-enhanced solid-state NMR spectroscopy of chromatin polymers.Journal of magnetic resonance open · 2022Article
- Transient RNA Interactions Leave a Covalent Imprint on a Viral Capsid Protein.Journal of the American Chemical Society · 2022Article
- Conformational Dynamics of Light-Harvesting Complex II in a Native Membrane Environment.Biophysical journal · 2021Article
- Competing Transfer Pathways in Direct and Indirect Dynamic Nuclear Polarization MAS NMR Experiments on HIV-1 Capsid Assemblies: Implications for Sensitivity and Resolution.Magnetic resonance (Gottingen, Germany) · 2021Article
- Targetable Tetrazine-Based Dynamic Nuclear Polarization Agents for Biological Systems.Chembiochem : a European journal of chemical biology · 2020Article
- Non-uniform sampling in quantitative assessment of heterogeneous solid-state NMR line shapes.Journal of biomolecular NMR · 2020Article
- Modulation of Transmembrane Domain Interactions in Neu Receptor Tyrosine Kinase by Membrane Fluidity and Cholesterol.The Journal of membrane biology · 2019Article
- Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies.The journal of physical chemistry. B · 2019Article
- Article
- Fast detection and structural identification of carbocations on zeolites by dynamic nuclear polarization enhanced solid-state NMR.Chemical science · 2018Article
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- N,N-Diethylmethylamine as lineshape standard for NMR above 130 K.Journal of magnetic resonance (San Diego, Calif. : 1997) · 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
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100 K. Protein dynamics are poorly understood below the freezing point of water and down to liquid nitrogen temperatures. Therefore, we investigate the α-spectrin SH3 domain by magic angle spinning (MAS) solid state NMR (ssNMR) at various temperatures while cooling slowly. Cooling down to 95 K, the NMR-signals of SH3 first broaden and at lower temperatures they separate into several peaks. The coalescence temperature differs depending on the individual residue. The broadening is shown to be inhomogeneous by hole-burning experiments. The coalescence behavior of 26 resolved signals (of 62) was compared to water proximity and crystal structure Debye-Waller factors (B-factors). Close proximity to the solvent and large B-factors (i.e. mobility) lead, generally, to a higher coalescence temperature. We interpret a high coalescence temperature as indicative of a large number of magnetically inequivalent populations at cryogenic temperature.
Indexed as
Identifiers
21826519What 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.