ArticleProceedings of the National Academy of Sciences of the United States of America1999
Mechanical and chemical unfolding of a single protein: a comparison.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 351 papers.
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Who cites it
351 citing papers in PubMed.
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- Assessment of the Adhesion to Decellularized Cardiac Patches of Stem Cells Through Single-Cell Force Spectroscopy (SCFS).Biomimetics (Basel, Switzerland) · 2026Article
- The Minimal Folding Motif of the Repeat-in-Toxin Domain of Adenylate Cyclase Toxin.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Computational design of superstable proteins through maximized hydrogen bonding.Nature chemistry · 2026Article
- Multiple modes of AFM reveal distinct mechanical properties for dystrophin and utrophin not manifest by small fragments.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The local mechanostructural properties of protein cargoes regulate nucleocytoplasmic transport.Nature physics · 2026Article
- Genetically encoded mechano-sensors with versatile readouts and compact size.bioRxiv : the preprint server for biology · 2025Article
- Viscoelasticity of a single poly-protein probed step-by-step during its mechanical unfolding and refolding under the force-clamp conditions.RSC advances · 2025Article
- Article
- Structural Basis of High-Precision Protein Ligation and Its Application.Journal of the American Chemical Society · 2025Article
- Pulling Forces Differentially Affect Refolding Pathways Due to Entangled Misfolded States in SARS-CoV-1 and SARS-CoV-2 Receptor Binding Domain.Biomolecules · 2024Article
- Parsing digital or analog TCR performance through piconewton forces.Science advances · 2024Article
- The strongest protein binder is surprisingly labile.Protein science : a publication of the Protein Society · 2024Article
- Two operational modes of atomic force microscopy reveal similar mechanical properties for homologous regions of dystrophin and utrophin.bioRxiv : the preprint server for biology · 2024Article
- Structural anisotropy results in mechano-directional transport of proteins across nuclear pores.Nature physics · 2024Article
- Enzyme-less nanopore detection of post-translational modifications within long polypeptides.Nature nanotechnology · 2023Article
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- Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease.Cell reports · 2023Article
- PEGylated Polymeric Nanoparticles Loaded with 2-Methoxyestradiol for the Treatment of Uterine Leiomyoma in a Patient-Derived Xenograft Mouse Model.Journal of pharmaceutical sciences · 2023Article
- Folding-unfolding asymmetry and aRoyal Society open science · 2023Article
291 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Is the mechanical unraveling of protein domains by atomic force microscopy (AFM) just a technological feat or a true measurement of their unfolding? By engineering a protein made of tandem repeats of identical Ig modules, we were able to get explicit AFM data on the unfolding rate of a single protein domain that can be accurately extrapolated to zero force. We compare this with chemical unfolding rates for untethered modules extrapolated to 0 M denaturant. The unfolding rates obtained by the two methods are the same. Furthermore, the transition state for unfolding appears at the same position on the folding pathway when assessed by either method. These results indicate that mechanical unfolding of a single protein by AFM does indeed reflect the same event that is observed in traditional unfolding experiments. The way is now open for the extensive use of AFM to measure folding reactions at the single-molecule level. Single-molecule AFM recordings have the added advantage that they define the reaction coordinate and expose rare unfolding events that cannot be observed in the absence of chemical denaturants.
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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.