ArticleProtein science : a publication of the Protein Society2006
Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 50 citations in OpenAlex.
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- Fob1 and Fob2 Proteins Are Virulence Determinants of Rhizopus oryzae via Facilitating Iron Uptake from Ferrioxamine.PLoS pathogens · 2015Article
- Mapping membrane protein backbone dynamics: a comparison of site-directed spin labeling with NMR 15N-relaxation measurements.Biophysical journal · 2014Article
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- High throughput platforms for structural genomics of integral membrane proteins.Current opinion in structural biology · 2011Review
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Mixing and matching detergents for membrane protein NMR structure determination.Journal of the American Chemical Society · 2009Article
- Backbone structure of a small helical integral membrane protein: A unique structural characterization.Protein science : a publication of the Protein Society · 2009Article
- Efficient cell-free production of olfactory receptors: detergent optimization, structure, and ligand binding analyses.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Investigation of the utility of selective methyl protonation for determination of membrane protein structures.Journal of biomolecular NMR · 2008Article
- Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634.Protein science : a publication of the Protein Society · 2008Article
- Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better.Biochimica et biophysica acta · 2007Review
- A high-throughput method for membrane protein solubility screening: the ultracentrifugation dispersity sedimentation assay.Protein science : a publication of the Protein Society · 2007Article
- Cell-free complements in vivo expression of the E. coli membrane proteome.Protein science : a publication of the Protein Society · 2007Article
- Comparative analysis and "expression space" coverage of the production of prokaryotic membrane proteins for structural genomics.Protein science : a publication of the Protein Society · 2006Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Structural studies of integral membrane proteins typically rely upon detergent micelles as faithful mimics of the native lipid bilayer. Therefore, membrane protein structure determination would be greatly facilitated by biophysical techniques that are capable of evaluating and assessing the fold and oligomeric state of these proteins solubilized in detergent micelles. In this study, an approach to the characterization of detergent-solubilized integral membrane proteins is presented. Eight Thermotoga maritima membrane proteins were screened for solubility in 11 detergents, and the resulting soluble protein-detergent complexes were characterized with small angle X-ray scattering (SAXS), nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD) spectroscopy, and chemical cross-linking to evaluate the homogeneity, oligomeric state, radius of gyration, and overall fold. A new application of SAXS is presented, which does not require density matching, and NMR methods, typically used to evaluate soluble proteins, are successfully applied to detergent-solubilized membrane proteins. Although detergents with longer alkyl chains solubilized the most proteins, further characterization indicates that some of these protein-detergent complexes are not well suited for NMR structure determination due to conformational exchange and protein oligomerization. These results emphasize the need to screen several different detergents and to characterize the protein-detergent complex in order to pursue structural studies. Finally, the physical characterization of the protein-detergent complexes indicates optimal solution conditions for further structural studies for three of the eight overexpressed membrane proteins.
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