ArticleEuropean biophysics journal : EBJ2013
Amphipol-assisted folding of bacteriorhodopsin in the presence or absence of lipids: functional consequences.
Article in European biophysics journal : EBJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Changes in Membrane Protein Structural Biology.Biology · 2020Review
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Determining the amphipol distribution within membrane-protein fibre samples using small-angle neutron scattering.Acta crystallographica. Section D, Structural biology · 2018Article
- Saposin Lipid Nanoparticles: A Highly Versatile and Modular Tool for Membrane Protein Research.Structure (London, England : 1993) · 2018Article
- Light-independent phospholipid scramblase activity of bacteriorhodopsin from Halobacterium salinarum.Scientific reports · 2017Article
- Reversible Unfolding of Rhomboid Intramembrane Proteases.Biophysical journal · 2016Article
- Solution behavior and crystallization of cytochrome bc₁ in the presence of amphipols.The Journal of membrane biology · 2014Article
- 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
- Amphipol-mediated screening of molecular orthoses specific for membrane protein targets.The Journal of membrane biology · 2014Article
- Amphipols and photosynthetic light-harvesting pigment-protein complexes.The Journal of membrane biology · 2014Article
- High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase.The Journal of membrane biology · 2014Article
- Amphipols for each season.The Journal of membrane biology · 2014Review
- How amphipols embed membrane proteins: global solvent accessibility and interaction with a flexible protein terminus.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
- Amphipols in G protein-coupled receptor pharmacology: what are they good for?The Journal of membrane biology · 2014Review
- The use of amphipols for NMR structural characterization of 7-TM proteins.The Journal of membrane biology · 2014Article
- Molecular dynamics simulations of a membrane protein/amphipol complex.The Journal of membrane biology · 2014Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amphipols are short amphipathic polymers designed to stabilize membrane proteins in aqueous solutions in the absence of detergent. Bacteriorhodopsin (BR), a light-driven proton pump, has been denatured, either by direct solubilization of the purple membrane in sodium dodecylsulfate (SDS) solution or by a procedure that involves delipidation with organic solvent followed by transfer to SDS, and renatured in amphipol A8-35. The effect of different renaturation procedures and of the presence or absence of lipids and the cofactor retinal have been investigated. The resulting samples have been characterized by absorbance spectroscopy, size-exclusion chromatography, thermostability measurements, and determination of photocycle kinetics. Transfer to A8-35 can be achieved by SDS precipitation, dilution, or dialysis, the first route resulting in the highest yield of refolding. Functional BR can be refolded whether in the presence or absence of lipids, higher yields being achieved in their presence. Retinal is not required for the protein to refold, but it stabilizes the refolded form and, thereby, improves folding yields. Lipids are not required for BR to perform its complete photocycle, but their presence speeds up the return to the ground state. Taken together, these data indicate that a membrane or membrane-mimetic environment is not required for correct decoding of the chemical information contained in the sequence of BR; functional folding is possible even in the highly foreign environment of lipid-free amphipols. BR interactions with lipids, however, contribute to an effective photocycle.
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