ArticleJournal of the American Chemical Society2011
Highly anisotropic stability and folding kinetics of a single coiled coil protein under mechanical tension.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 67 citations in OpenAlex.
- Autoregressive HMM resolves biomolecular transitions from passive optical tweezer force measurements.Biophysical journal · 2025Article
- Genetically encoded mechano-sensors with versatile readouts and compact size.bioRxiv : the preprint server for biology · 2025Article
- How SNARE proteins generate force to fuse membranes.Biophysical journal · 2025Article
- Digital and Tunable Genetically Encoded Tension Sensors Based on Engineered Coiled-Coils.Angewandte Chemie (International ed. in English) · 2025Article
- Coiled-coil domains are sufficient to drive liquid-liquid phase separation in protein models.Biophysical journal · 2024Article
- Unveiling Mechanical Activation: GAIN Domain Unfolding and Dissociation in Adhesion GPCRs.Nano letters · 2023Article
- Force redistribution in clathrin-mediated endocytosis revealed by coiled-coil force sensors.Science advances · 2023Article
- Coiled-coil domains are sufficient to drive liquid-liquid phase separation of proteins in molecular models.bioRxiv : the preprint server for biology · 2023Article
- Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022Review
- Force Dependence of Proteins' Transition State Position and the Bell-Evans Model.Nanomaterials (Basel, Switzerland) · 2021Article
- Evidence for S2 flexibility by direct visualization of quantum dot-labeled myosin heads and rods within smooth muscle myosin filaments moving on actin in vitro.The Journal of general physiology · 2021Article
- Studying heat shock proteins through single-molecule mechanical manipulation.Cell stress & chaperones · 2020Review
- Bio-Molecular Applications of Recent Developments in Optical Tweezers.Biomolecules · 2019Review
- Molecular mechanics of coiled coils loaded in the shear geometry.Chemical science · 2018Article
- Multiplexed fluctuation-dissipation-theorem calibration of optical tweezers inside living cells.The Review of scientific instruments · 2017Article
- Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Protein science : a publication of the Protein Society · 2017Review
- Single-Molecule Protein Folding Experiments Using High-Precision Optical Tweezers.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Hidden Markov Modeling with Detailed Balance and Its Application to Single Protein Folding.Biophysical journal · 2016Article
- A simple DNA handle attachment method for single molecule mechanical manipulation experiments.Protein science : a publication of the Protein Society · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Coiled coils are one of the most abundant protein structural motifs and widely mediate protein interactions and force transduction or sensation. They are thus model systems for protein engineering and folding studies, particularly the GCN4 coiled coil. Major single-molecule methods have also been applied to this protein and revealed its folding kinetics at various spatiotemporal scales. Nevertheless, the folding energy and the kinetics of a single GCN4 coiled coil domain have not been well determined at a single-molecule level. Here we used high-resolution optical tweezers to characterize the folding and unfolding reactions of a single GCN4 coiled coil domain and their dependence on the pulling direction. In one axial and two transverse pulling directions, we observed reversible, two-state transitions of the coiled coil in real time. The transitions equilibrate at pulling forces ranging from 6 to 12 pN, showing different stabilities of the coiled coil in regard to pulling direction. Furthermore, the transition rates vary with both the magnitude and the direction of the pulling force by greater than 1000 folds, indicating a highly anisotropic and topology-dependent energy landscape for protein transitions under mechanical tension. We developed a new analytical theory to extract energy and kinetics of the protein transition at zero force. The derived folding energy does not depend on the pulling direction and is consistent with the measurement in bulk, which further confirms the applicability of the single-molecule manipulation approach for energy measurement. The highly anisotropic thermodynamics of proteins under tension should play important roles in their biological functions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.