ArticleThe journal of physical chemistry. B2009
Temperature and chemical denaturant dependence of forced unfolding of titin I27.
Article in The journal of physical chemistry. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
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Who cites it
12 citing papers in PubMed.
- Mechanically weak and highly dynamic state of mechanosensitive titin Ig domains induced by proline isomerization.Nature communications · 2025Article
- Analytical methods in studying cell force sensing: principles, current technologies and perspectives.Regenerative biomaterials · 2025Review
- Tandem repeats of highly bioluminescent NanoLuc are refolded noncanonically by the Hsp70 machinery.Protein science : a publication of the Protein Society · 2024Article
- Correlation between chemical denaturation and the unfolding energetics of Acanthamoeba actophorin.Biophysical journal · 2023Article
- Temperature dependent mechanical unfolding and refolding of a protein studied by thermo-regulated optical tweezers.Biophysical journal · 2023Article
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Folding pathway of an Ig domain is conserved on and off the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Titin-Based Nanoparticle Tension Sensors Map High-Magnitude Integrin Forces within Focal Adhesions.Nano letters · 2016Article
- Multiscale mechanobiology: mechanics at the molecular, cellular, and tissue levels.Cell & bioscience · 2013Article
- Computational investigation of the effect of thermal perturbation on the mechanical unfolding of titin I27.Journal of molecular modeling · 2012Article
- Direct quantification of the attempt frequency determining the mechanical unfolding of ubiquitin protein.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Single-molecule force measurement opens a new door for investigating detailed biomolecular interactions and their thermodynamic properties by pulling molecules apart while monitoring the force exerted on them. Recent advances in the nonequilibrium work theorem allows one to determine the free-energy landscapes of these events. Such information is valuable for understanding processes such as protein and RNA folding and receptor-ligand binding. Here, we used force as a physical parameter under the traditional chemical and temperature denaturing environment to alter the protein folding energy landscape and compared the change in the unfolding free-energy barrier of the I27 domain of human cardiac titin. We found that the trends in protein unfolding free-energy barriers are consistent for single-molecule force measurements and bulk chemical and temperature studies. The results suggest that the information from single-molecule pulling experiments are meaningful and useful for understanding the mechanism of folding of titin I27.
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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.