ArticleJournal of the American Chemical Society2016
Picosecond Photobiology: Watching a Signaling Protein Function in Real Time via Time-Resolved Small- and Wide-Angle X-ray Scattering.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 35 citations in OpenAlex.
- A light-triggered Time-Resolved X-ray Solution Scattering (TR-XSS) workflow with application to protein conformational dynamics.FEBS open bio · 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
- Time-resolved x-ray solution scattering from detergent solubilized visual rhodopsin.Biophysical journal · 2026Article
- Absolute scaling of small- and wide-angle X-ray scattering images recorded with short duration X-ray pulses on a large area fiber-taper X-ray detector.Journal of synchrotron radiation · 2026Article
- Unfolding of the Villin Headpiece Domain: Revealing Structural Heterogeneity with Time-Resolved X-Ray Solution Scattering and Markov State Modeling.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- Early Folding Dynamics of i-Motif DNA Revealed by pH-Jump Time-Resolved X-ray Solution Scattering.Journal of the American Chemical Society · 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
- Watching a signaling protein function: What has been learned over four decades of time-resolved studies of photoactive yellow protein.Structural dynamics (Melville, N.Y.) · 2024Review
- BioCARS: Synchrotron facility for probing structural dynamics of biological macromolecules.Structural dynamics (Melville, N.Y.) · 2024Article
- Sample-minimizing co-flow cell for time-resolved pump-probe X-ray solution scattering.Journal of synchrotron radiation · 2023Article
- The Role of Transient Intermediate Structures in the Unfolding of the Trp-Cage Fast-Folding Protein: Generating Ensembles from Time-Resolved X-ray Solution Scattering with Genetic Algorithms.The journal of physical chemistry letters · 2023Article
- A setup for millisecond time-resolved X-ray solution scattering experiments at the CoSAXS beamline at the MAX IV Laboratory.Journal of synchrotron radiation · 2022Article
- Tracking the ATP-binding response in adenylate kinase in real time.Science advances · 2021Article
- Using photocaging for fast time-resolved structural biology studies.Acta crystallographica. Section D, Structural biology · 2021Review
- Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.Cell reports. Physical science · 2021Article
- Unfolding bovine α-lactalbumin with T-jump: Characterizing disordered intermediates via time-resolved x-ray solution scattering and molecular dynamics simulations.The Journal of chemical physics · 2021Article
- Pump-Probe Circular Dichroism Spectroscopy of Cyanobacteriochrome TePixJ Yields: Insights into Its Photoconversion.The journal of physical chemistry. B · 2021Article
- Integrating solvation shell structure in experimentally driven molecular dynamics using x-ray solution scattering data.The Journal of chemical physics · 2020Article
- Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme.Nature chemistry · 2019Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
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 at 4 institutions in 1 country.
Funding
Abstract
The capacity to respond to environmental changes is crucial to an organism's survival. Halorhodospira halophila is a photosynthetic bacterium that swims away from blue light, presumably in an effort to evade photons energetic enough to be genetically harmful. The protein responsible for this response is believed to be photoactive yellow protein (PYP), whose chromophore photoisomerizes from trans to cis in the presence of blue light. We investigated the complete PYP photocycle by acquiring time-resolved small and wide-angle X-ray scattering patterns (SAXS/WAXS) over 10 decades of time spanning from 100 ps to 1 s. Using a sequential model, global analysis of the time-dependent scattering differences recovered four intermediates (pR0/pR1, pR2, pB0, pB1), the first three of which can be assigned to prior time-resolved crystal structures. The 1.8 ms pB0 to pB1 transition produces the PYP signaling state, whose radius of gyration (Rg = 16.6 Å) is significantly larger than that for the ground state (Rg = 14.7 Å) and is therefore inaccessible to time-resolved protein crystallography. The shape of the signaling state, reconstructed using GASBOR, is highly anisotropic and entails significant elongation of the long axis of the protein. This structural change is consistent with unfolding of the 25 residue N-terminal domain, which exposes the β-scaffold of this sensory protein to a potential binding partner. This mechanistically detailed description of the complete PYP photocycle, made possible by time-resolved crystal and solution studies, provides a framework for understanding signal transduction in proteins and for assessing and validating theoretical/computational approaches in protein biophysics.
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.