ArticleThe journal of physical chemistry letters2016
Reconciling Intermediates in Mechanical Unfolding Experiments with Two-State Protein Folding in Bulk.
Article in The journal of physical chemistry letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Strain learning in protein-based mechanical metamaterials.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein.Communications chemistry · 2021Article
- Review
- Diverse Folding Pathways of HIV-1 Protease Monomer on a Rugged Energy Landscape.Biophysical journal · 2019Article
- The influence of disulfide bonds on the mechanical stability of proteins is context dependent.The Journal of biological chemistry · 2017Article
- Proteins Breaking Bad: A Free Energy Perspective.The journal of physical chemistry letters · 2017Article
- Competing Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase.Biophysical journal · 2017Article
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2 authors.
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Abstract
Most experimentally well-characterized single domain proteins of less than 100 residues have been found to be two-state folders. That is, only two distinct populations can explain both equilibrium and kinetic measurements. Results from single molecule force spectroscopy, where a protein is unfolded by applying a mechanical pulling force to its ends, have largely confirmed this description for proteins found to be two-state in ensemble experiments. Recently, however, stable intermediates have been reported in mechanical unfolding experiments on a cold-shock protein previously found to be a prototypical two-state folder. Here, we tackle this discrepancy using free energy landscapes and Markov state models derived from coarse-grained molecular simulations. We show that protein folding intermediates can be selectively stabilized by the pulling force and that the populations of these intermediates vary in a force-dependent manner. Our model qualitatively captures the experimental results and suggests a possible origin of the apparent discrepancy.
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