ArticleNature communications2016
A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026Article
- Molecular dynamics simulations reveal DNA gate opening mechanisms for M. smegmatis topoisomerase 1A.Biophysical journal · 2026Article
- GenUnfold: Rapidly Predict Protein Mechanical Unfolding Trajectory via a Physics-Guided Diffusion Model.Proceedings of machine learning research · 2026Article
- A Type III secretion system effector evolved to be mechanically labile and initiate unfolding from the N-terminus.bioRxiv : the preprint server for biology · 2026Article
- Effect of Additional Terminal Residues on the Folding and Unfolding Dynamics of Cold Shock Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mapping cryptic phosphorylation sites in the human proteome.The EMBO journal · 2025Article
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Exploring force-driven stochastic folding dynamics in mechano-responsive proteins and implications in phenotypic variation.Nature communications · 2025Article
- Identical sequences, different behaviors: Protein diversity captured at the single-molecule level.Biophysical journal · 2024Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Using steered molecular dynamic tension for assessing quality of computational protein structure models.Journal of computational chemistry · 2022Article
- Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein.Communications chemistry · 2021Article
- Review
- Highly Dynamic Polynuclear Metal Cluster Revealed in a Single Metallothionein Molecule.Research (Washington, D.C.) · 2021Article
- Disordered proteins follow diverse transition paths as they fold and bind to a partner.Science (New York, N.Y.) · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- On the Interpretation of Force-Induced Unfolding Studies of Membrane Proteins Using Fast Simulations.Biophysical journal · 2019Article
- Diverse Folding Pathways of HIV-1 Protease Monomer on a Rugged Energy Landscape.Biophysical journal · 2019Article
- Multistep Protein Unfolding Scenarios from the Rupture of a Complex Metal Cluster CdScientific reports · 2019Article
- Fodis: Software for Protein Unfolding Analysis.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A major drive in protein folding has been to develop experimental technologies to resolve the myriads of microscopic pathways and complex mechanisms that purportedly underlie simple two-state folding behaviour. This is key for cross-validating predictions from theory and modern computer simulations. Detecting such complexity experimentally has remained elusive even using methods with improved time, structural or single-molecule resolution. Here, we investigate the mechanical unfolding of cold shock protein B (Csp), a showcase two-state folder, using single-molecule force-spectroscopy. Under controlled-moderate pulling forces, the unfolding of Csp emerges as highly heterogeneous with trajectories ranging from single sweeps to different combinations of multiple long-lived mechanical intermediates that also vary in order of appearance. Steered molecular dynamics simulations closely reproduce the experimental observations, thus matching unfolding patterns with structural events. Our results provide a direct glimpse at the nanoscale complexity underlying two-state folding, and postulate these combined methods as unique tools for dissecting the mechanical unfolding mechanisms of such proteins.
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