ArticleStructural dynamics (Melville, N.Y.)2020
Real-time tracking of protein unfolding with time-resolved x-ray solution scattering.
Article in Structural dynamics (Melville, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 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
- A Bayesian Approach to Interpret Time-Resolved Experiments Using Molecular Simulations.ACS physical chemistry Au · 2026Article
- A new reference for changes in X-ray scattering from water due to temperature changes at ambient conditions.Journal of synchrotron radiation · 2026Article
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
- Emerging ultrafast technologies in biotechnology.3 Biotech · 2025Review
- Emerging Time-Resolved X-Ray Diffraction Approaches for Protein Dynamics.Annual review of biophysics · 2023Review
- 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
- Resolving Dynamics in the Ensemble: Finding Paths through Intermediate States and Disordered Protein Structures.The journal of physical chemistry. B · 2021Article
- Time-resolved X-ray scattering studies of proteins.Current opinion in structural biology · 2021Review
- The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature.Acta crystallographica. Section D, Structural biology · 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
- Real-time tracking of protein unfolding with time-resolved x-ray solution scattering.Structural dynamics (Melville, N.Y.) · 2020Article
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Authors and funding
8 authors.
Funding
Abstract
The correct folding of proteins is of paramount importance for their function, and protein misfolding is believed to be the primary cause of a wide range of diseases. Protein folding has been investigated with time-averaged methods and time-resolved spectroscopy, but observing the structural dynamics of the unfolding process in real-time is challenging. Here, we demonstrate an approach to directly reveal the structural changes in the unfolding reaction. We use nano- to millisecond time-resolved x-ray solution scattering to probe the unfolding of apomyoglobin. The unfolding reaction was triggered using a temperature jump, which was induced by a nanosecond laser pulse. We demonstrate a new strategy to interpret time-resolved x-ray solution scattering data, which evaluates ensembles of structures obtained from molecular dynamics simulations. We find that apomyoglobin passes three states when unfolding, which we characterize as native, molten globule, and unfolded. The molten globule dominates the population under the conditions investigated herein, whereas native and unfolded structures primarily contribute before the laser jump and 30
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