ArticleNpj biosensing2024
Energy landscape of conformational changes for a single unmodified protein.
Article in Npj biosensing, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Label-Free Single Protein Dynamics Revealed by Metasurface-Enhanced Raman Spectroscopy.ACS nano · 2026Article
- Plasmonic Optical Tweezers and Surface-Enhanced Raman Spectroscopy: Fundamentals, Single-Entity Applications, and the Evolving Role of Artificial Intelligence.Bioengineering (Basel, Switzerland) · 2026Review
- Vibrational contribution to the sub-terahertz dielectric response of kinesin and its hydration shell.Scientific reports · 2026Article
- Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.Journal of chemical theory and computation · 2026Article
- Label-Free Single-Molecule Conalbumin Analysis.Micromachines · 2026Article
- Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins.Npj biosensing · 2026Article
- Direct observation of small molecule activator binding to single PR65 protein.Npj biosensing · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resolving the free energy landscapes that govern protein biophysics has been obscured by ensemble averaging. While the folding dynamics of single proteins have been observed using fluorescent labels and/or tethers, a simpler and more direct measurement of the conformational changes would not require modifications to the protein. We use nanoaperture optical tweezers to resolve the energy landscape of a single unmodified protein, Bovine Serum Albumin (BSA), and quantify changes in the three-state conformation dynamics with temperature. A Markov model with Kramers' theory transition rates is used to model the dynamics, showing good agreement with the observed state transitions. This first look at the intrinsic energy landscape of proteins provides a transformative tool for protein biophysics and may be applied broadly, including mapping out the energy landscape of particularly challenging intrinsically disordered proteins.
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.