ArticleBiophysical journal2012
Single-molecule experiments reveal the flexibility of a Per-ARNT-Sim domain and the kinetic partitioning in the unfolding pathway under force.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein.Communications chemistry · 2021Article
- Protein folding mechanism revealed by single-molecule force spectroscopy experiments.Biophysics reports · 2021Article
- An ester bond underlies the mechanical strength of a pathogen surface protein.Nature communications · 2021Article
- Reconstruction of ARNT PAS-B Unfolding Pathways by Steered Molecular Dynamics and Artificial Neural Networks.Journal of chemical theory and computation · 2021Article
- Fragile protein folds: Sequence and environmental factors affecting the equilibrium of two interconverting, stably folded protein conformations.Magnetic resonance (Gottingen, Germany) · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Broken force dispersal network in tip-links by the mutations at the CaThe Biochemical journal · 2019Article
- Differences in the mechanical unfolding pathways of apo- and copper-bound azurins.Scientific reports · 2018Article
- Investigations of the CLOCK and BMAL1 Proteins Binding to DNA: A Molecular Dynamics Simulation Study.PloS one · 2016Article
- The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins.Nature communications · 2015Article
- Force-induced remodelling of proteins and their complexes.Current opinion in structural biology · 2015Review
- Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin.Nature communications · 2014Article
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7 authors.
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Abstract
Per-ARNT-Sim (PAS) domains serve as versatile binding motifs in many signal-transduction proteins and are able to respond to a wide spectrum of chemical or physical signals. Despite their diverse functions, PAS domains share a conserved structure. It has been suggested that the structure of PAS domains is flexible and thus adaptable to many binding partners. However, direct measurement of the flexibility of PAS domains has not yet been provided. Here, we quantitatively measure the mechanical unfolding of a PAS domain, ARNT PAS-B, using single-molecule atomic force microscopy. Our force spectroscopy results indicate that the structure of ARNT PAS-B can be unraveled under mechanical forces as low as ~30 pN due to its broad potential well for the mechanical unfolding transition of ~2 nm. This allows the PAS-B domain to extend by up to 75% of its resting end-to-end distance without unfolding. Moreover, we found that the ARNT PAS-B domain unfolds in two distinct pathways via a kinetic partitioning mechanism. Sixty-seven percent of ARNT PAS-B unfolds through a simple two-state pathway, whereas the other 33% unfolds with a well-defined intermediate state in which the C-terminal β-hairpin is detached. We propose that the structural flexibility and force-induced partial unfolding of PAS-B domains may provide a unique mechanism for them to recruit diverse binding partners and lower the free-energy barrier for the formation of the binding interface.
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