ArticleBiochemistry2014
Detergent optimized membrane protein reconstitution in liposomes for solid state NMR.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- A direct solubilization approach to purify active full-length human neuropathy target esterase.Protein expression and purification · 2025Article
- Proteomic analysis of the urothelial cancer landscape.Nature communications · 2024Article
- A Fluorescence-based Approach Utilizing Self-labeling Enzyme Tags to Determine Protein Orientation in Large Unilamellar Vesicles.Bio-protocol · 2022Article
- Tools shaping drug discovery and development.Biophysics reviews · 2022Review
- Single Vesicle Fluorescence-Bleaching Assay for Multi-Parameter Analysis of Proteoliposomes by Total Internal Reflection Fluorescence Microscopy.ACS applied materials & interfaces · 2022Article
- Identification of the salusin-β receptor using proteoliposomes embedded with endogenous membrane proteins.Scientific reports · 2018Article
- Optimization of Detergent-Mediated Reconstitution of Influenza A M2 Protein into Proteoliposomes.Membranes · 2018Article
- Structural Influences: Cholesterol, Drug, and Proton Binding to Full-Length Influenza A M2 Protein.Biophysical journal · 2016Article
- Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies.Frontiers in molecular biosciences · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
For small helical membrane proteins, their structures are highly sensitive to their environment, and solid state NMR is a structural technique that can characterize these membrane proteins in native-like lipid bilayers and proteoliposomes. To date, a systematic method by which to evaluate the effect of the solubilizing detergent on proteoliposome preparations for solid state NMR of membrane proteins has not been presented in the literature. A set of experiments are presented aimed at determining the conditions most amenable to dialysis mediated reconstitution sample preparation. A membrane protein from M. tuberculosis is used to illustrate the method. The results show that a detergent that stabilizes the most protein is not always ideal and sometimes cannot be removed by dialysis. By focusing on the lipid and protein binding properties of the detergent, proteoliposome preparations can be readily produced, which provide double the signal-to-noise ratios for both the oriented sample and magic angle spinning solid state NMR. The method will allow more membrane protein drug targets to be structurally characterized in lipid bilayer environments.
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Registered trials
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