ArticleBiochemistry2010
Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 56 citations in OpenAlex.
- In situ analysis of osmolyte mechanisms of proteome thermal stabilization.Nature chemical biology · 2024Article
- Understanding the Modulation of α-Synuclein Fibrillation byACS omega · 2024Article
- The variable domain from dynamin-related protein 1 promotes liquid-liquid phase separation that enhances its interaction with cardiolipin-containing membranes.Protein science : a publication of the Protein Society · 2023Article
- A Thermodynamic Atlas of Proteomes Reveals Energetic Innovation across the Tree of Life.Molecular biology and evolution · 2022Article
- Review
- A theoretical study on the effects of interdomain flexibility on drug encounter rate for coronavirus nucleocapsid-type proteins.Biophysical chemistry · 2021Article
- Taurine Induces an Ordered but Functionally Inactive Conformation in Intrinsically Disordered Casein Proteins.Scientific reports · 2020Article
- Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo.Cellular and molecular life sciences : CMLS · 2018Review
- Folding and Lipid Composition Determine Membrane Interaction of the Disordered Protein COR15A.Biophysical journal · 2018Article
- Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein.Biophysical journal · 2018Article
- Conditionally disordered proteins: bringing the environment back into the fold.Cellular and molecular life sciences : CMLS · 2017Review
- Folding propensity of intrinsically disordered proteins by osmotic stress.Molecular bioSystems · 2016Article
- Electrostatic Energetics of Bacillus subtilis Ribonuclease P Protein Determined by Nuclear Magnetic Resonance-Based Histidine pKa Measurements.Biochemistry · 2015Article
- Conformational kinetics reveals affinities of protein conformational states.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Forced folding of a disordered protein accesses an alternative folding landscape.Chemphyschem : a European journal of chemical physics and physical chemistry · 2015Article
- Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).Molecular & cellular proteomics : MCP · 2014Article
- Ligand concentration regulates the pathways of coupled protein folding and binding.Journal of the American Chemical Society · 2014Article
- Protein domain definition should allow for conditional disorder.Protein science : a publication of the Protein Society · 2013Article
- Structural insights into the folding defects of oncogenic pVHL lead to correction of its function in vitro.PloS one · 2013Article
- Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Understanding the interconversion between thermodynamically distinguishable states present in a protein folding pathway provides not only the kinetics and energetics of protein folding but also insights into the functional roles of these states in biological systems. The protein component of the bacterial RNase P holoenzyme from Bacillus subtilis (P protein) was previously shown to be unfolded in the absence of its cognate RNA or other anionic ligands. P protein was used in this study as a model system to explore general features of intrinsically disordered protein (IDP) folding mechanisms. The use of trimethylamine N-oxide (TMAO), an osmolyte that stabilizes the unliganded folded form of the protein, enabled us to study the folding process of P protein in the absence of ligand. Transient stopped-flow kinetic traces at various final TMAO concentrations exhibited multiphasic kinetics. Equilibrium "cotitration" experiments were performed using both TMAO and urea during the titration to produce a urea-TMAO titration surface of P protein. Both kinetic and equilibrium studies show evidence of a previously undetected intermediate state in the P protein folding process. The intermediate state is significantly populated, and the folding rate constants are relatively slow compared to those of intrinsically folded proteins similar in size and topology. The experiments and analysis described serve as a useful example for mechanistic folding studies of other IDPs.
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.