ArticleProceedings of the National Academy of Sciences of the United States of America2009
Direct evidence for a dry molten globule intermediate during the unfolding of a small protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- The Nature of Non-Arrhenius Kinetics in the Heat Denaturation of Proteins.International journal of molecular sciences · 2026Article
- The Arch from the Stones: Understanding Protein Folding Energy Landscapes via Bioinspired Collective Variables.The journal of physical chemistry letters · 2025Article
- Thirty years of StAR gazing. Expanding the universe of the steroidogenic acute regulatory protein.The Journal of endocrinology · 2025Review
- Dry molten globule conformational state of CYP11A1 (SCC) regulates the first step of steroidogenesis in the mitochondrial matrix.iScience · 2024Article
- Photoradical-Mediated Catalyst-Independent Protein Cross-Link with Unusual Fluorescence Properties.Chembiochem : a European journal of chemical biology · 2023Article
- Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins.International journal of molecular sciences · 2023Review
- Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein.Protein science : a publication of the Protein Society · 2022Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception.Molecules (Basel, Switzerland) · 2022Review
- Protein folding - seeing is deceiving.Protein science : a publication of the Protein Society · 2021Article
- α-Synuclein aggregation nucleates through liquid-liquid phase separation.Nature chemistry · 2020Article
- Structure of an Unfolding Intermediate of an RRM Domain of ETR-3 Reveals Its Native-like Fold.Biophysical journal · 2020Article
- Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.Biomolecules · 2019Review
- Article
- Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein.eLife · 2019Article
- Fast pressure-jump all-atom simulations and experiments reveal site-specific protein dehydration-folding dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- CcdB at pH 4 Forms a Partially Unfolded State with a Dry Core.Biophysical journal · 2019Article
- Structural effects of methylglyoxal glycation, a study on the model protein MNEI.Molecular and cellular biochemistry · 2019Article
- Article
- Aggregation-primed molten globule conformers of the p53 core domain provide potential tools for studying p53C aggregation in cancer.The Journal of biological chemistry · 2018Article
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Little is known about how proteins begin to unfold. In particular, how and when water molecules penetrate into the protein interior during unfolding, thereby enabling the dissolution of specific structure, is poorly understood. The hypothesis that the native state expands initially into a dry molten globule, in which tight packing interactions are broken, but whose hydrophobic core has not expanded sufficiently to be able to absorb water molecules, has very little experimental support. Here, we report our analysis of the earliest observable events during the unfolding of single chain monellin (MNEI), a small plant protein. Far- and near-UV circular dichroism measurements of GdnHCl-induced unfolding indicate that a molten globule intermediate forms initially, before the major slow unfolding reaction commences. Steady-state fluorescence resonance energy transfer measurements show that the C-terminal end of the single helix of MNEI initially moves rapidly away from the single tryptophan residue that is close to the N-terminal end of the helix. The average end-to-end distance of the protein also expands during unfolding to the molten globule intermediate. At this time, water has yet to penetrate the protein core, according to the evidence from intrinsic tryptophan fluorescence and 8-anilino-1-naphthalenesulfonic acid fluorescence-monitored kinetic unfolding measurements. Our results therefore provide direct evidence for a dry molten globule intermediate at the initial stage of unfolding. Our results further suggest that the structural transition between the native and dry molten globule states could be an all-or-none transition, whereas further swelling of the globule appears to occur gradually.
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