ArticleNanotechnology2017
Multidomain proteins under force.
Article in Nanotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed.
- Building block aspect ratio controls assembly, architecture, and mechanics of synthetic and natural protein networks.Nature communications · 2023Article
- Mechanical regulation of talin through binding and history-dependent unfolding.Science advances · 2022Article
- Optimal Sacrificial Domains in Mechanical Polyproteins:JACS Au · 2022Article
- Quantitative Elasticity of Flexible Polymer Chains Using Interferometer-Based AFM.Nanomaterials (Basel, Switzerland) · 2022Article
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Cation-induced shape programming and morphing in protein-based hydrogels.Science advances · 2020Article
- Chemical unfolding of protein domains induces shape change in programmed protein hydrogels.Nature communications · 2019Article
- The molecular mechanisms underlying mussel adhesion.Nanoscale advances · 2019Review
- The extracellular matrix-myosin pathway in mechanotransduction: from molecule to tissue.Emerging topics in life sciences · 2018Article
- Force-Clamp Rheometry for Characterizing Protein-based Hydrogels.Journal of visualized experiments : JoVE · 2018Article
- Mechanical Deformation Accelerates Protein Ageing.Angewandte Chemie (International ed. in English) · 2017Article
- Proteins Breaking Bad: A Free Energy Perspective.The journal of physical chemistry letters · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Advancements in single-molecule force spectroscopy techniques such as atomic force microscopy and magnetic tweezers allow investigation of how domain folding under force can play a physiological role. Combining these techniques with protein engineering and HaloTag covalent attachment, we investigate similarities and differences between four model proteins: I10 and I91-two immunoglobulin-like domains from the muscle protein titin, and two α + β fold proteins-ubiquitin and protein L. These proteins show a different mechanical response and have unique extensions under force. Remarkably, when normalized to their contour length, the size of the unfolding and refolding steps as a function of force reduces to a single master curve. This curve can be described using standard models of polymer elasticity, explaining the entropic nature of the measured steps. We further validate our measurements with a simple energy landscape model, which combines protein folding with polymer physics and accounts for the complex nature of tandem domains under force. This model can become a useful tool to help in deciphering the complexity of multidomain proteins operating under force.
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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.