ArticleNature communications2011
Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein.
Article in Nature communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed.
- Many Ways Out: Beyond the Two-State Model of Protein Unfolding.ACS omega · 2026Review
- The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking.Nature structural & molecular biology · 2025Article
- Single molecule spectrum dynamics imaging with 3D target-locking tracking.Nature communications · 2025Article
- Multiplexed Single-Molecule Detection of Nucleic Acid Biomarkers with a Distance-Tuned Single FRET Pair.Analytical chemistry · 2025Article
- Review
- Data-driven probabilistic definition of the low energy conformational states of protein residues.NAR genomics and bioinformatics · 2024Article
- An encompassed representation of timescale hierarchies in first-order reaction network.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A billion years of evolution manifest in nanosecond protein dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Folding pathway of a discontinuous two-domain protein.Nature communications · 2024Article
- Trends in Single-Molecule Total Internal Reflection Fluorescence Imaging and Their Biological Applications with Lab-on-a-Chip Technology.Sensors (Basel, Switzerland) · 2023Review
- Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates.Nature communications · 2023Article
- An Efficient Path Classification Algorithm Based on Variational Autoencoder to Identify Metastable Path Channels for Complex Conformational Changes.Journal of chemical theory and computation · 2023Article
- Endocytosis-Like Vesicle Fission Mediated by a Membrane-Expanding Molecular Machine Enables Virus Encapsulation for In Vivo Delivery.Journal of the American Chemical Society · 2023Article
- Frustration and the Kinetic Repartitioning Mechanism of Substrate Inhibition in Enzyme Catalysis.The journal of physical chemistry. B · 2022Article
- TDP-43 drives synaptic and cognitive deterioration following traumatic brain injury.Acta neuropathologica · 2022Article
- Cooperativity and Folding Kinetics in a Multidomain Protein with Interwoven Chain Topology.ACS central science · 2022Article
- Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Unraveling multi-state molecular dynamics in single-molecule FRET experiments. I. Theory of FRET-lines.The Journal of chemical physics · 2022Article
- Theory and Analysis of Single-Molecule FRET Experiments.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins.Methods (San Diego, Calif.) · 2021Article
23 more citing papers are in PubMed but not listed here.
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7 authors.
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Abstract
Proteins attain their function only after folding into a highly organized three-dimensional structure. Much remains to be learned about the mechanisms of folding of large multidomain proteins, which may populate metastable intermediate states on their energy landscapes. Here we introduce a novel method, based on high-throughput single-molecule fluorescence experiments, which is specifically geared towards tracing the dynamics of folding in the presence of a plethora of intermediates. We employ this method to characterize the folding reaction of a three-domain protein, adenylate kinase. Using thousands of single-molecule trajectories and hidden Markov modelling, we identify six metastable states on adenylate kinase's folding landscape. Remarkably, the connectivity of the intermediates depends on denaturant concentration; at low concentration, multiple intersecting folding pathways co-exist. We anticipate that the methodology introduced here will find broad applicability in the study of folding of large proteins, and will provide a more realistic scenario of their conformational dynamics.
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