ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structure of a transient protein-folding intermediate by pressure-jump NMR spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Many Ways Out: Beyond the Two-State Model of Protein Unfolding.ACS omega · 2026Review
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.Journal of the American Chemical Society · 2026Article
- Making invisible excited-state structures of pro-interleukin-18 visible by combining NMR and machine learning.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.bioRxiv : the preprint server for biology · 2026Article
- Structure of a transient protein-folding intermediate by pressure-jump NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Protein folding, as commonly portrayed, involves exploration of a rough, high-dimensional landscape, ending with a final descent into a low-energy folded state. During that journey, the protein may visit shallow basins corresponding to metastable structures, potentially of biological importance. Structural characterization of transiently populated metastable states is challenging due to their low population, which limits traditional NMR, and also makes crystallization for X-ray diffraction difficult without stabilizing mutations, covalent modifications, or the addition of antibodies. Here, we report the structural characterization of the on-pathway folding intermediate of a pressure-sensitized ubiquitin mutant. The obtained non-native β-sheet registry was previously shown to be necessary in the PINK1 mitophagy pathway. We used fast pressure jumps to repeatedly initiate folding and advanced NMR measurements to probe the evolving ensemble of protein conformations. The results reported here demonstrate that the non-native β-sheet hydrogen bond registry can act as a metastable trap during protein folding. This work provides a template for future investigation of metastable conformations and protein folding with rich structural detail.
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