ArticleNanoscale2020
Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly.
Article in Nanoscale, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed.
- Modification of Whey Protein Isolate with Surfactants Based on Hofmeister Series and Interaction Parameter.ACS omega · 2026Article
- A Redefined Protocol for Protein Corona Analysis on Graphene Oxide.ACS nanoscience Au · 2025Article
- Proximity labeling of axonemal protein CFAP91 identifies EFCAB5 that regulates sperm motility.Nature communications · 2025Article
- Biodegradation of Zearalenone by a NovelMicroorganisms · 2025Article
- SDS Depletion from Intact Membrane Proteins by KCl Precipitation Ahead of Mass Spectrometry Analysis.Proteomes · 2025Article
- Prospects and challenges of recombinant spider venom enzymes: insights fromFrontiers in bioengineering and biotechnology · 2025Article
- Biological Detoxification of Aflatoxin BFoods (Basel, Switzerland) · 2024Article
- Investigating the effects of ultrafine bubbles on bacterial growth.RSC advances · 2024Article
- Impact of covalent binding with p-coumaric acid on pea protein's structural and functional properties.Current research in food science · 2024Article
- Transmembrane Helices 7 and 8 Confer Aggregation Sensitivity to the Cystic Fibrosis Transmembrane Conductance Regulator.International journal of molecular sciences · 2023Article
- Allergies Come Clean: The Role of Detergents in Epithelial Barrier Dysfunction.Current allergy and asthma reports · 2023Review
- Benchmarking Molecular Dynamics Force Fields for All-Atom Simulations of Biological Condensates.Journal of chemical theory and computation · 2023Article
- In-Vial Detection of Protein Denaturation Using Intrinsic Fluorescence Anisotropy.Analytical chemistry · 2023Article
- Improving Both the Thermostability and Catalytic Efficiency of Phospholipase D fromInternational journal of molecular sciences · 2022Article
- Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure.Molecules (Basel, Switzerland) · 2022Article
- Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Controllable enzymatic superactivity of α-chymotrypsin activated by the electrostatic interaction with cationic gemini surfactants.RSC advances · 2021Article
- An integrative toolbox to unlock the structure and dynamics of protein-surfactant complexes.Nanoscale advances · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The effects of detergent sodium dodecyl sulfate (SDS) on protein structure and dynamics are fundamental to the most common laboratory technique used to separate proteins and determine their molecular weights: polyacrylamide gel electrophoresis. However, the mechanism by which SDS induces protein unfolding and the microstructure of protein-SDS complexes remain largely unknown. Here, we report a detailed account of SDS-induced unfolding of two proteins-I27 domain of titin and β-amylase-obtained through all-atom molecular dynamics simulations. Both proteins were found to spontaneously unfold in the presence of SDS at boiling water temperature on the time scale of several microseconds. The protein unfolding was found to occur via two distinct mechanisms in which specific interactions of individual SDS molecules disrupt the protein's secondary structure. In the final state of the unfolding process, the proteins are found to wrap around SDS micelles in a fluid necklace-and-beads configuration, where the number and location of bound micelles changes dynamically. The global conformation of the protein was found to correlate with the number of SDS micelles bound to it, whereas the number of SDS molecules directly bound to the protein was found to define the relaxation time scale of the unfolded protein. Our microscopic characterization of SDS-protein interactions sets the stage for future refinement of SDS-enabled protein characterization methods, including protein fingerprinting and sequencing using a solid-state nanopore.
Indexed as
Identifiers
What Socratic 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 Socratic graph.