ArticleProceedings of the National Academy of Sciences of the United States of America2012
The molten globule state is unusually deformable under mechanical force.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
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- Pulling Forces Differentially Affect Refolding Pathways Due to Entangled Misfolded States in SARS-CoV-1 and SARS-CoV-2 Receptor Binding Domain.Biomolecules · 2024Article
- Catch bonds in sickle cell disease: Shear-enhanced adhesion of red blood cells to laminin.Biophysical journal · 2023Article
- Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding.Molecules (Basel, Switzerland) · 2023Review
- Direct observation of chemo-mechanical coupling in DnaK by single-molecule force experiments.Biophysical journal · 2022Article
- A look at the face of the molten globule: Structural model of the Helicobacter pylori apoflavodoxin ensemble at acidic pH.Protein science : a publication of the Protein Society · 2022Article
- New insights into the folding-unfolding mechanism and conformations of cytochrome C.Chemical science · 2022Article
- Molten globule-like transition state of protein barnase measured with calorimetric force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein folding mechanism revealed by single-molecule force spectroscopy experiments.Biophysics reports · 2021Article
- Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis.Nanomaterials (Basel, Switzerland) · 2021Article
- Force transduction creates long-ranged coupling in ribosomes stalled by arrest peptides.Biophysical journal · 2021Article
- Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.Biophysical journal · 2020Article
- Synthesis runs counter to directional folding of a nascent protein domain.Nature communications · 2020Article
- Studying heat shock proteins through single-molecule mechanical manipulation.Cell stress & chaperones · 2020Review
- Non-equilibrium dynamics of a nascent polypeptide during translation suppress its misfolding.Nature communications · 2019Article
- Bio-Molecular Applications of Recent Developments in Optical Tweezers.Biomolecules · 2019Review
- Switching of the folding-energy landscape governs the allosteric activation of protein kinase A.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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4 authors.
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Abstract
Recently, the role of force in cellular processes has become more evident, and now with advances in force spectroscopy, the response of proteins to force can be directly studied. Such studies have found that native proteins are brittle, and thus not very deformable. Here, we examine the mechanical properties of a class of intermediates referred to as the molten globule state. Using optical trap force spectroscopy, we investigated the response to force of the native and molten globule states of apomyoglobin along different pulling axes. Unlike natively folded proteins, the molten globule state of apomyoglobin is compliant (large distance to the transition state); this large compliance means that the molten globule is more deformable and the unfolding rate is more sensitive to force (the application of force or tension will have a more dramatic effect on the unfolding rate). Our studies suggest that these are general properties of molten globules and could have important implications for mechanical processes in the cell.
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