ArticleJournal of the American Chemical Society2013
Nanomechanics of HaloTag tethers.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- A PET reporter ligand for quantitative imaging of gene expression in the brain.Nature biomedical engineering · 2026Article
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- From viral assembly to host interaction: AFM's contributions to virology.Journal of virology · 2025Review
- Identical sequences, different behaviors: Protein diversity captured at the single-molecule level.Biophysical journal · 2024Article
- The Bioimaging Story of AIEgens.Chemical & biomedical imaging · 2023Review
- Chemical tags and beyond: Live-cell protein labeling technologies for modern optical imaging.Smart molecules : open access · 2023Review
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- One-step asparaginyl endopeptidase (RSC chemical biology · 2022Article
- Article
- Nonexponential kinetics captured in sequential unfolding of polyproteins over a range of loads.Current research in structural biology · 2022Article
- Microbial production of megadalton titin yields fibers with advantageous mechanical properties.Nature communications · 2021Article
- DsbA is a redox-switchable mechanical chaperone.Chemical science · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Protein folding modulates the chemical reactivity of a Gram-positive adhesin.Nature chemistry · 2021Article
- Mechanical Stability of a Small, Highly-Luminescent Engineered Protein NanoLuc.International journal of molecular sciences · 2020Article
- HaloFlippers: A General Tool for the Fluorescence Imaging of Precisely Localized Membrane Tension Changes in Living Cells.ACS central science · 2020Article
- Power to the protein: enhancing and combining activities using the Spy toolbox.Chemical science · 2020Review
- Stretching DNA to twice the normal length with single-molecule hydrodynamic trapping.Lab on a chip · 2020Article
- A HaloTag-TEV genetic cassette for mechanical phenotyping of proteins from tissues.Nature communications · 2020Article
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Authors and funding
8 authors.
Funding
Abstract
The active site of the Haloalkane Dehydrogenase (HaloTag) enzyme can be covalently attached to a chloroalkane ligand providing a mechanically strong tether, resistant to large pulling forces. Here we demonstrate the covalent tethering of protein L and I27 polyproteins between an atomic force microscopy (AFM) cantilever and a glass surface using HaloTag anchoring at one end and thiol chemistry at the other end. Covalent tethering is unambiguously confirmed by the observation of full length polyprotein unfolding, combined with high detachment forces that range up to ∼2000 pN. We use these covalently anchored polyproteins to study the remarkable mechanical properties of HaloTag proteins. We show that the force that triggers unfolding of the HaloTag protein exhibits a 4-fold increase, from 131 to 491 pN, when the direction of the applied force is changed from the C-terminus to the N-terminus. Force-clamp experiments reveal that unfolding of the HaloTag protein is twice as sensitive to pulling force compared to protein L and refolds at a slower rate. We show how these properties allow for the long-term observation of protein folding-unfolding cycles at high forces, without interference from the HaloTag tether.
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Registered trials
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.