ArticleNature chemistry2019
Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme.
Article in Nature chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed.
- A light-triggered Time-Resolved X-ray Solution Scattering (TR-XSS) workflow with application to protein conformational dynamics.FEBS open bio · 2026Article
- Generalizing the Gaussian Network Model: Spanning-Tree Thermodynamics Shows Entropy-Driven KRAS Activation.Proteins · 2026Article
- A Bayesian Approach to Interpret Time-Resolved Experiments Using Molecular Simulations.ACS physical chemistry Au · 2026Article
- Assessing protein-specific radiation damage in time-resolved X-ray solution-scattering experiments at high-brilliance synchrotrons using fast detector readout.Acta crystallographica. Section D, Structural biology · 2026Article
- A new reference for changes in X-ray scattering from water due to temperature changes at ambient conditions.Journal of synchrotron radiation · 2026Article
- Temporal ghost imaging for pump-probe X-ray solution scattering.Acta crystallographica. Section A, Foundations and advances · 2025Article
- Structure-Based Experimental Datasets for Benchmarking Protein Simulation Force Fields [Article v1.0].Living journal of computational molecular science · 2025Article
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
- Kinetics and dynamics of oligonucleotide hybridization.Nature reviews. Chemistry · 2025Review
- Macromolecular crystallography and biology at the Linac Coherent Light Source.Journal of synchrotron radiation · 2025Article
- Time-resolved X-ray solution scattering unveils the events leading to hemoglobin heme capture by staphylococcal IsdB.Nature communications · 2025Article
- Predicting absolute protein folding stability using generative models.Protein science : a publication of the Protein Society · 2025Article
- 3D variability analysis reveals a hidden conformational change controlling ammonia transport in human asparagine synthetase.Nature communications · 2024Article
- 3D Variability Analysis Reveals a Hidden Conformational Change Controlling Ammonia Transport in Human Asparagine Synthetase.bioRxiv : the preprint server for biology · 2024Article
- Unlocking the unfolded structure of ubiquitin: Combining time-resolved x-ray solution scattering and molecular dynamics to generate unfolded ensembles.The Journal of chemical physics · 2024Article
- Article
- Activation and friction in enzymatic loop opening and closing dynamics.Nature communications · 2024Article
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Microsecond dynamics control the HIV-1 Envelope conformation.Science advances · 2024Article
- BioCARS: Synchrotron facility for probing structural dynamics of biological macromolecules.Structural dynamics (Melville, N.Y.) · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Correlated motions of proteins are critical to function, but these features are difficult to resolve using traditional structure determination techniques. Time-resolved X-ray methods hold promise for addressing this challenge, but have relied on the exploitation of exotic protein photoactivity, and are therefore not generalizable. Temperature jumps, through thermal excitation of the solvent, have been utilized to study protein dynamics using spectroscopic techniques, but their implementation in X-ray scattering experiments has been limited. Here, we perform temperature-jump small- and wide-angle X-ray scattering measurements on a dynamic enzyme, cyclophilin A, demonstrating that these experiments are able to capture functional intramolecular protein dynamics on the microsecond timescale. We show that cyclophilin A displays rich dynamics following a temperature jump, and use the resulting time-resolved signal to assess the kinetics of conformational changes. Two relaxation processes are resolved: a fast process is related to surface loop motions, and a slower process is related to motions in the core of the protein that are critical for catalytic turnover.
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.