ArticleProceedings of the National Academy of Sciences of the United States of America2014
How force unfolding differs from chemical denaturation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
28 citing papers in PubMed.
- Embrace Disorder as a Function: Bio-Informed Biomaterials Design Advanced by Intrinsically Disordered Proteins.Biomimetics (Basel, Switzerland) · 2026Article
- Single-molecule mechanostructural fingerprinting of nucleic acid conformations.Nucleic acids research · 2026Article
- Stabilising large biologics through complimentary buffer component protection and rapid drying times.International journal of pharmaceutics: X · 2025Article
- A direct computational assessment of vinculin-actin unbinding kinetics reveals catch-bonding behavior.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Dithiol Based on l-Cysteine and Cysteamine as a Disulfide-Reducing Agent.The Journal of organic chemistry · 2022Article
- Measuring biological materials mechanics with atomic force microscopy - Mechanical unfolding of biopolymers.Microscopy research and technique · 2022Article
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- Protons Are Fast and Smart; Proteins Are Slow and Dumb: On the Relationship of Electrospray Ionization Charge States and Conformations.Journal of the American Society for Mass Spectrometry · 2021Article
- Tungsten Oxide Nanodots Exhibit Mild Interactions with WW and SH3 Modular Protein Domains.ACS omega · 2020Article
- Differences in stability and calcium sensitivity of the Ig domains in titin's N2A region.Protein science : a publication of the Protein Society · 2020Article
- Mechanical Unfolding of Spectrin Repeats Induces Water-Molecule Ordering.Biophysical journal · 2020Article
- Modeling protein folding in vivo.Biology direct · 2018Article
- Rare Dissipative Transitions Punctuate the Initiation of Chemical Denaturation in Proteins.Biophysical journal · 2018Article
- Exploring the Denatured State Ensemble by Single-Molecule Chemo-Mechanical Unfolding: The Effect of Force, Temperature, and Urea.Journal of molecular biology · 2018Article
- The force-dependent mechanism of DnaK-mediated mechanical folding.Science advances · 2018Article
- The Role of Controlled Surface Topography and Chemistry on Mouse Embryonic Stem Cell Attachment, Growth and Self-Renewal.Materials (Basel, Switzerland) · 2017Article
- Graphene-Induced Pore Formation on Cell Membranes.Scientific reports · 2017Article
- Probing conformational dynamics of an enzymatic active site by an in situ single fluorogenic probe under piconewton force manipulation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Probing Small Molecule Binding to Unfolded Polyprotein Based on its Elasticity and Refolding.Biophysical journal · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Single-molecule force spectroscopies are remarkable tools for studying protein folding and unfolding, but force unfolding explores protein configurations that are potentially very different from the ones traditionally explored in chemical or thermal denaturation. Understanding these differences is crucial because such configurations serve as starting points of folding studies, and thus can affect both the folding mechanism and the kinetics. Here we provide a detailed comparison of both chemically induced and force-induced unfolded state ensembles of ubiquitin based on extensive, all-atom simulations of the protein either extended by force or denatured by urea. As expected, the respective unfolded states are very different on a macromolecular scale, being fully extended under force with no contacts and partially extended in urea with many nonnative contacts. The amount of residual secondary structure also differs: A significant population of α-helices is found in chemically denatured configurations but such helices are absent under force, except at the lowest applied force of 30 pN where short helices form transiently. We see that typical-size helices are unstable above this force, and β-sheets cannot form. More surprisingly, we observe striking differences in the backbone dihedral angle distributions for the protein unfolded under force and the one unfolded by denaturant. A simple model based on the dialanine peptide is shown to not only provide an explanation for these striking differences but also illustrates how the force dependence of the protein dihedral angle distributions give rise to the worm-like chain behavior of the chain upon force.
Indexed as
Identifiers
What OpenQuestion holds
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.