ReviewBiochimica et biophysica acta2010
A method for solution NMR structural studies of large integral membrane proteins: reverse micelle encapsulation.
Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 30 citations in OpenAlex.
- Ligandability at the Membrane Interface of GPx4 Revealed through a Reverse Micelle Fragment Screening Platform.JACS Au · 2024Article
- Ligandability at the membrane interface of GPx4 revealed through a reverse micelle fragment screening platform.bioRxiv : the preprint server for biology · 2024Article
- Solution NMR investigations of integral membrane proteins: Challenges and innovations.Current opinion in structural biology · 2023Review
- Reverse Micelle Encapsulation of Proteins for NMR Spectroscopy.Methods in enzymology · 2019Article
- Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Archives of biochemistry and biophysics · 2014Review
- High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Reverse micelles as a tool for probing solvent modulation of protein dynamics: Reverse micelle encapsulated hemoglobin.Chemical physics · 2013Article
- HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation.Journal of molecular biology · 2011Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The structural study of membrane proteins perhaps represents one of the greatest challenges of the post-genomic era. While membrane proteins comprise over 50% of current and potential drug targets, their structural characterization lags far behind that of soluble proteins. Nuclear magnetic resonance (NMR) offers great potential not only with respect to structural characterization of integral membrane proteins but may also provide the ability to study the details of small ligand interactions. However, the size limitations of solution NMR have restricted comprehensive structural characterization of membrane protein NMR structures to the relatively small beta-barrel proteins or helical proteins of relatively simple topology. In an effort to escape the barriers presented by slow molecular reorientation of large integral membrane proteins solubilized by detergent micelles in water, we have adapted the reverse micelle encapsulation strategy originally developed for the study of large soluble proteins by solution NMR methods. Here we review a novel approach to the solubilization of large integral membrane proteins in reverse micelle surfactants dissolved in low viscosity alkane solvents. The procedure is illustrated with a 54kDa construct of the homotetrameric KcsA potassium channel.
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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 OpenQuestion graph.