ArticleThe Journal of membrane biology2014
How amphipols embed membrane proteins: global solvent accessibility and interaction with a flexible protein terminus.
Article in The Journal of membrane biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 34 citations in OpenAlex.
- Characterizing the Specific Recognition of Xanthurenic Acid by GEP1 and GEP1-GCα Interactions in cGMP Signaling Pathway in Gametogenesis of Malaria Parasites.International journal of molecular sciences · 2023Article
- Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.Biomolecules · 2022Review
- The Det.Belt Server: A Tool to Visualize and Estimate Amphipathic Solvent Belts around Membrane Proteins.Membranes · 2021Article
- Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017Review
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- NMR as a tool to investigate the structure, dynamics and function of membrane proteins.Nature structural & molecular biology · 2016Article
- Long-term stability of a vaccine formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis.The Journal of membrane biology · 2014Article
- Isolation of Escherichia coli mannitol permease, EIImtl, trapped in amphipol A8-35 and fluorescein-labeled A8-35.The Journal of membrane biology · 2014Article
- Amphipols for each season.The Journal of membrane biology · 2014Review
- Amphipol-mediated screening of molecular orthoses specific for membrane protein targets.The Journal of membrane biology · 2014Article
- Synthesis, characterization and applications of a perdeuterated amphipol.The Journal of membrane biology · 2014Article
- Thermal fluctuations in amphipol A8-35 particles: a neutron scattering and molecular dynamics study.The Journal of membrane biology · 2014Article
- Nanoparticle surface-enhanced Raman scattering of bacteriorhodopsin stabilized by amphipol A8-35.The Journal of membrane biology · 2014Article
- Amphipols and photosynthetic light-harvesting pigment-protein complexes.The Journal of membrane biology · 2014Article
- The use of amphipols for solution NMR studies of membrane proteins: advantages and constraints as compared to other solubilizing media.The Journal of membrane biology · 2014Article
- Labeling and functionalizing amphipols for biological applications.The Journal of membrane biology · 2014Review
- Application of amphipols for structure-functional analysis of TRP channels.The Journal of membrane biology · 2014Review
- Molecular dynamics simulations of a membrane protein/amphipol complex.The Journal of membrane biology · 2014Article
- Solution behavior and crystallization of cytochrome bc₁ in the presence of amphipols.The Journal of membrane biology · 2014Article
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amphipathic polymers called amphipols provide a valuable alternative to detergents for keeping integral membrane proteins soluble in aqueous buffers. Here, we characterize spatial contacts of amphipol A8-35 with membrane proteins from two architectural classes: The 8-stranded β-barrel outer membrane protein OmpX and the α-helical protein bacteriorhodopsin. OmpX is well structured in A8-35, with its barrel adopting a fold closely similar to that in dihexanoylphosphocholine micelles. The accessibility of A8-35-trapped OmpX by a water-soluble paramagnetic molecule is highly similar to that in detergent micelles and resembles the accessibility in the natural membrane. For the α-helical protein bacteriorhodopsin, previously shown to keep its fold and function in amphipols, NMR data show that the imidazole protons of a polyhistidine tag at the N-terminus of the protein are exchange protected in the presence of detergent and lipid bilayer nanodiscs, but not in amphipols, indicating the absence of an interaction in the latter case. Overall, A8-35 exhibits protein interaction properties somewhat different from detergents and lipid bilayer nanodiscs, while maintaining the structure of solubilized integral membrane proteins.
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