ArticleNature communications2016
Subnanometre enzyme mechanics probed by single-molecule force spectroscopy.
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 34 papers.
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Who cites it
34 citing papers in PubMed.
- Single Molecule Force Measurements Reveal Energy Stabilization of Theophylline Aptamer RNA Switch Required for Gene Control.ACS physical chemistry Au · 2026Article
- Allosteric regulation of enzymatic catalysis by molecular crowding.Communications chemistry · 2026Article
- Visualize Transient Water-Mediated Hydrogen Bonds Facilitating the Formation of Enzymatic Near-Attack Conformers.JACS Au · 2025Article
- Article
- On the distance to the transition state of protein folding in optical tweezers experiments.Biophysical reviews · 2025Review
- Prediction of the Stability of Protein Substructures Using AI/ML Techniques.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Allostery can convert binding free energies into concerted domain motions in enzymes.Nature communications · 2024Article
- Article
- Whispering-Gallery Mode Optoplasmonic Microcavities: From Advanced Single-Molecule Sensors and Microlasers to Applications in Synthetic Biology.ACS photonics · 2024Review
- Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate byBiochemistry · 2023Article
- Direct observation of chemo-mechanical coupling in DnaK by single-molecule force experiments.Biophysical journal · 2022Article
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Visualizing Intramolecular Dynamics of Membrane Proteins.International journal of molecular sciences · 2022Review
- Frustration and the Kinetic Repartitioning Mechanism of Substrate Inhibition in Enzyme Catalysis.The journal of physical chemistry. B · 2022Article
- Cooperativity and Folding Kinetics in a Multidomain Protein with Interwoven Chain Topology.ACS central science · 2022Article
- Mechanics of CRISPR-Cas12a and engineered variants on λ-DNA.Nucleic acids research · 2022Article
- ADP-Induced Conformational Transition of Human Adenylate Kinase 1 Is Triggered by Suppressing Internal Motion of αBiomolecules · 2022Article
- Article
- Detection of weak non-covalent cation-π interactions in NGAL by single-molecule force spectroscopy.Nano research · 2022Article
- Classifying Residues in Mechanically Stable and Unstable Substructures Based on a Protein Sequence: The Case Study of the DnaK Hsp70 Chaperone.Nanomaterials (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes are molecular machines that bind substrates specifically, provide an adequate chemical environment for catalysis and exchange products rapidly, to ensure fast turnover rates. Direct information about the energetics that drive conformational changes is difficult to obtain. We used subnanometre single-molecule force spectroscopy to study the energetic drive of substrate-dependent lid closing in the enzyme adenylate kinase. Here we show that in the presence of the bisubstrate inhibitor diadenosine pentaphosphate (AP5A), closing and opening of both lids is cooperative and tightly coupled to inhibitor binding. Surprisingly, binding of the substrates ADP and ATP exhibits a much smaller energetic drive towards the fully closed state. Instead, we observe a new dominant energetic minimum with both lids half closed. Our results, combining experiment and molecular dynamics simulations, give detailed mechanical insights into how an enzyme can cope with the seemingly contradictory requirements of rapid substrate exchange and tight closing, to ensure efficient catalysis.
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