ArticleJournal of biomolecular NMR2010
Cell-free expression and stable isotope labelling strategies for membrane proteins.
Article in Journal of biomolecular NMR, 2010. 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, 82 citations in OpenAlex.
- Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis.Communications biology · 2022Article
- Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.RSC chemical biology · 2021Review
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- Amino-acid selective isotope labeling enables simultaneous overlapping signal decomposition and information extraction from NMR spectra.Journal of biomolecular NMR · 2020Article
- Expression and purification of recombinant G protein-coupled receptors: A review.Protein expression and purification · 2020Review
- CombLabel: rational design of optimized sequence-specific combinatorial labeling schemes. Application to backbone assignment of membrane proteins with low stability.Journal of biomolecular NMR · 2019Article
- Article
- From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins.Structure (London, England : 1993) · 2016Article
- Stable isotope labeling strategy based on coding theory.Journal of biomolecular NMR · 2015Article
- Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015Review
- An extended combinatorial 15N, 13Cα, and 13C' labeling approach to protein backbone resonance assignment.Journal of biomolecular NMR · 2015Article
- Time-shared experiments for efficient assignment of triple-selectively labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Selective (15)N-labeling of the side-chain amide groups of asparagine and glutamine for applications in paramagnetic NMR spectroscopy.Journal of biomolecular NMR · 2014Article
- Advances in NMR structures of integral membrane proteins.Current opinion in structural biology · 2013Review
- Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment.Journal of biomolecular NMR · 2012Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- Solution NMR structure of proteorhodopsin.Angewandte Chemie (International ed. in English) · 2011Article
- A rapid and robust method for selective isotope labeling of proteins.Methods (San Diego, Calif.) · 2011Article
- Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O.Journal of biomolecular NMR · 2011Article
- An economical method for producing stable-isotope labeled proteins by the E. coli cell-free system.Journal of biomolecular NMR · 2010Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins are highly underrepresented in the structural data-base and remain one of the most challenging targets for functional and structural elucidation. Their roles in transport and cellular communication, furthermore, often make over-expression toxic to their host, and their hydrophobicity and structural complexity make isolation and reconstitution a complicated task, especially in cases where proteins are targeted to inclusion bodies. The development of cell-free expression systems provides a very interesting alternative to cell-based systems, since it circumvents many problems such as toxicity or necessity for the transportation of the synthesized protein to the membrane, and constitutes the only system that allows for direct production of membrane proteins in membrane-mimetic environments which may be suitable for liquid state NMR measurements. The unique advantages of the cell-free expression system, including strong expression yields as well as the direct incorporation of almost any combination of amino acids with very little metabolic scrambling, has allowed for the development of a wide-array of isotope labelling techniques which facilitate structural investigations of proteins whose spectral congestion and broad line-widths may have earlier rendered them beyond the scope of NMR. Here we explore various labelling strategies in conjunction with cell-free developments, with a particular focus on alpha-helical transmembrane proteins which benefit most from such methods.
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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.