ArticleBiophysical journal2009
Mechanical characterization of protein L in the low-force regime by electromagnetic tweezers/evanescent nanometry.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed.
- Protein force spectroscopy using magnetic tweezers: Slow and steady wins the race?Biophysical journal · 2026Review
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.Protein science : a publication of the Protein Society · 2024Article
- Single-molecule magnetic tweezers to probe the equilibrium dynamics of individual proteins at physiologically relevant forces and timescales.Nature protocols · 2024Review
- Identical sequences, different behaviors: Protein diversity captured at the single-molecule level.Biophysical journal · 2024Article
- Nonexponential kinetics captured in sequential unfolding of polyproteins over a range of loads.Current research in structural biology · 2022Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Multidomain proteins under force.Nanotechnology · 2017Article
- A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics.Journal of the American Chemical Society · 2016Article
- Mechano-adaptive sensory mechanism of α-catenin under tension.Scientific reports · 2016Article
- Work Done by Titin Protein Folding Assists Muscle Contraction.Cell reports · 2016Article
- Interrogating the activities of conformational deformed enzyme by single-molecule fluorescence-magnetic tweezers microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A dynamic DNA-repair complex observed by correlative single-molecule nanomanipulation and fluorescence.Nature structural & molecular biology · 2015Article
- The elastic free energy of a tandem modular protein under force.Biochemical and biophysical research communications · 2015Article
- Dynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces.Journal of the American Chemical Society · 2015Article
- Gold rotor bead tracking for high-speed measurements of DNA twist, torque and extension.Nature methods · 2014Article
- Electrically facilitated translocation of protein through solid nanopore.Nanoscale research letters · 2014Article
- Conformational plasticity of the essential membrane-associated mannosyltransferase PimA from mycobacteria.The Journal of biological chemistry · 2013Article
- Single molecule recordings of lysozyme activity.Physical chemistry chemical physics : PCCP · 2013Article
- Nanomechanics of HaloTag tethers.Journal of the American Chemical Society · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Mechanical manipulation at the single molecule level of proteins exhibiting mechanical stability poses a technical challenge that has been almost exclusively approached by atomic force microscopy (AFM) techniques. However, due to mechanical drift limitations, AFM techniques are restricted to experimental recordings that last less than a minute in the high-force regime. Here we demonstrate a novel combination of electromagnetic tweezers and evanescent nanometry that readily captures the forced unfolding trajectories of protein L at pulling forces as low as 10-15 pN. Using this approach, we monitor unfolding and refolding cycles of the same polyprotein for a period of time longer than 30 min. From such long-lasting recordings, we obtain ensemble averages of unfolding step sizes and rates that are consistent with single-molecule AFM data obtained at higher stretching forces. The unfolding kinetics of protein L at low stretching forces confirms and extends the observations that the mechanical unfolding rate is exponentially dependent on the pulling force within a wide range of stretching forces spanning from 13 pN up to 120 pN. Our experiments demonstrate a novel approach for the mechanical manipulation of single proteins for extended periods of time in the low-force regime.
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.