ArticleThe journal of physical chemistry. B2017
Quantification of Membrane Protein-Detergent Complex Interactions.
Article in The journal of physical chemistry. B, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 26 citations in OpenAlex.
- A Site-Specific Self-Association of a Protein Hub Drives Its Phase Separation.ACS chemical biology · 2026Article
- Real-Time Binding Kinetics of Membrane Protein-Protein Interactions in a Membraneless Setting.Analytical chemistry · 2025Article
- Single-Molecule Observation of Competitive Protein-Protein Interactions Utilizing a Nanopore.ACS nano · 2025Article
- Real-Time Measurement of a Weak Interaction of a Transcription Factor Motif with a Protein Hub at Single-Molecule Precision.ACS nano · 2024Article
- Convergent Alterations of a Protein Hub Produce Divergent Effects within a Binding Site.ACS chemical biology · 2022Article
- Current noise of a protein-selective biological nanopore.Proteomics · 2022Article
- The Det.Belt Server: A Tool to Visualize and Estimate Amphipathic Solvent Belts around Membrane Proteins.Membranes · 2021Article
- Kinetics of the multitasking high-affinity Win binding site of WDR5 in restricted and unrestricted conditions.The Biochemical journal · 2021Article
- Protein Ligand-Induced Amplification in the 1/Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Effects of Detergent on α-Synuclein Structure. A Native MS-Ion Mobility Study.International journal of molecular sciences · 2020Article
- Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly.Nanoscale · 2020Article
- Single-Molecule Protein Detection in a Biofluid Using a Quantitative Nanopore Sensor.ACS sensors · 2019Article
- High-Throughput Screening of Protein-Detergent Complexes Using Fluorescence Polarization Spectroscopy.Current protocols in protein science · 2019Article
- Structural and Functional Stability of DNA Nanopores in Biological Media.Nanomaterials (Basel, Switzerland) · 2019Article
- Rapid and Accurate Determination of Nanopore Ionic Current Using a Steric Exclusion Model.ACS sensors · 2019Article
- Kinetics of Membrane Protein-Detergent Interactions Depend on Protein Electrostatics.The journal of physical chemistry. B · 2018Article
- Detergent Desorption of Membrane Proteins Exhibits Two Kinetic Phases.The journal of physical chemistry letters · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
Although fundamentally significant in structural, chemical, and membrane biology, the interfacial protein-detergent complex (PDC) interactions have been modestly examined because of the complicated behavior of both detergents and membrane proteins in aqueous phase. Membrane proteins are prone to unproductive aggregation resulting from poor detergent solvation, but the participating forces in this phenomenon remain ambiguous. Here, we show that using rational membrane protein design, targeted chemical modification, and steady-state fluorescence polarization spectroscopy, the detergent desolvation of membrane proteins can be quantitatively evaluated. We demonstrate that depleting the detergent in the sample well produced a two-state transition of membrane proteins between a fully detergent-solvated state and a detergent-desolvated state, the nature of which depended on the interfacial PDC interactions. Using a panel of six membrane proteins of varying hydrophobic topography, structural fingerprint, and charge distribution on the solvent-accessible surface, we provide direct experimental evidence for the contributions of the electrostatic and hydrophobic interactions to the protein solvation properties. Moreover, all-atom molecular dynamics simulations report the major contribution of the hydrophobic forces exerted at the PDC interface. This semiquantitative approach might be extended in the future to include studies of the interfacial PDC interactions of other challenging membrane protein systems of unknown structure. This would have practical importance in protein extraction, solubilization, stabilization, and crystallization.
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.