ArticleProceedings of the National Academy of Sciences of the United States of America2009
Osmolyte-induced separation of the mechanical folding phases of ubiquitin.
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 16 papers.
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Who cites it
16 citing papers in PubMed, 54 citations in OpenAlex.
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function.Communications biology · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- The force-dependent mechanism of DnaK-mediated mechanical folding.Science advances · 2018Article
- Probing Small Molecule Binding to Unfolded Polyprotein Based on its Elasticity and Refolding.Biophysical journal · 2016Article
- Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates.Biophysical journal · 2016Article
- Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy.Nature protocols · 2013Article
- Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation.Biophysical journal · 2012Article
- Worm-like Ising model for protein mechanical unfolding under the effect of osmolytes.Biophysical journal · 2012Article
- Effects of pH on proteins: predictions for ensemble and single-molecule pulling experiments.Journal of the American Chemical Society · 2012Article
- Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy.Biophysical journal · 2011Article
- Protein folding at single-molecule resolution.Biochimica et biophysica acta · 2011Review
- Probing osmolyte participation in the unfolding transition state of a protein.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.The Journal of biological chemistry · 2010Article
- Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domains.The Journal of biological chemistry · 2010Article
- Understanding biology by stretching proteins: recent progress.Current opinion in structural biology · 2010Review
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Solvent molecules play key roles in the conformational dynamics of proteins. Here we use single molecule force-clamp spectroscopy to probe the role played by the stabilizing osmolyte glycerol on the conformational ensembles visited by a single ubiquitin protein folding after mechanical extension. Using a variety of force-pulse protocols, we find that glycerol stabilizes the native state of ubiquitin, making it more resistant to mechanical unfolding. We also find that although glycerol enhanced the hydrophobic collapse of unfolded and highly extended ubiquitins, it had no effect on the resulting collapsed states that are essential precursors of the folded state. These disparate effects of glycerol may be the result of distinct structural roles played by solvent molecules at the transition state of each folding ensemble. Our results open the way for a detailed analysis of the transition state structures that form along the folding trajectory of a mechanically extended protein.
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