ArticleBiophysical journal2021
Volume and compressibility differences between protein conformations revealed by high-pressure NMR.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Small Molecule Regulation of CLOCK:BMAL1 DNA Binding Activity.bioRxiv : the preprint server for biology · 2026Article
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- NMR data processing, visualization, analysis and structure calculation with NMRFx.Communications chemistry · 2025Article
- Pushed to extremes: distinct effects of high temperature versus pressure on the structure of STEP.Communications biology · 2024Article
- Non-uniform sampling of similar NMR spectra and its application to studies of the interaction between alpha-synuclein and liposomes.Journal of biomolecular NMR · 2023Article
- Pushed to extremes: distinct effects of high temperature vs. pressure on the structure of an atypical phosphatase.bioRxiv : the preprint server for biology · 2023Article
- Monitoring protein unfolding transitions by NMR-spectroscopy.Journal of biomolecular NMR · 2022Article
- Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure.The journal of physical chemistry. B · 2021Article
- High-pressure NMR measurements provide insights into the different structural states that proteins can adopt.Biophysical journal · 2021Article
- Fragile protein folds: Sequence and environmental factors affecting the equilibrium of two interconverting, stably folded protein conformations.Magnetic resonance (Gottingen, Germany) · 2021Article
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Abstract
Proteins often interconvert between different conformations in ways critical to their function. Although manipulating such equilibria for biophysical study is often challenging, the application of pressure is a potential route to achieve such control by favoring the population of lower volume states. Here, we use this feature to study the interconversion of ARNT PAS-B Y456T, which undergoes a dramatic +3 slip in the β-strand register as it switches between two stably folded conformations. Using high-pressure biomolecular NMR approaches, we obtained the first, to our knowledge, quantitative data testing two key hypotheses of this process: the slipped conformation is both smaller and less compressible than the wild-type equivalent, and the interconversion proceeds through a chiefly unfolded intermediate state. Data collected in steady-state pressure and time-resolved pressure-jump modes, including observed pressure-dependent changes in the populations of the two conformers and increased rate of interconversion between conformers, support both hypotheses. Our work exemplifies how these approaches, which can be generally applied to protein conformational switches, can provide unique information that is not easily accessible through other techniques.
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