G protein-coupled receptors (GPCRs) exhibit remarkable structural plasticity, which underlies their capacity to recognize a wide range of extracellular molecules and interact with intracellular partner proteins. Nuclear magnetic resonance (NMR) spectroscopy is uniquely well-suited to investigate GPCR structural plasticity, enabled by stable-isotope "probes" incorporated into receptors that inform on structure and dynamics. Progress with stable-isotope labeling methods in Eukaryotic expression...
[NMR paper] The transient expression of recombinant proteins in plant cell packs facilitates stable isotope labeling for NMR spectroscopy
The transient expression of recombinant proteins in plant cell packs facilitates stable isotope labeling for NMR spectroscopy
Nuclear magnetic resonance (NMR) spectroscopy can be used to determine the structure, dynamics and interactions of proteins. However, protein NMR requires stable isotope labeling for signal detection. The cells used for the production of recombinant proteins must therefore be grown in medium containing isotopically labeled substrates. Stable isotope labeling is well established in Escherichia coli, but bacteria are only suitable for the production of simple proteins...
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06-17-2022 08:24 AM
[NMR paper] G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling
G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling
G protein-coupled receptors (GPCRs) are a large membrane protein family found in higher organisms, including the human body. GPCRs mediate cellular responses to diverse extracellular stimuli and thus control key physiological functions, which makes them important targets for drug design. Signaling by GPCRs is related to the structure and dynamics of these proteins, which are modulated by extrinsic ligands as well as by...
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05-15-2022 06:54 AM
[NMR paper] Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR.
Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR.
Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR.
J Phys Chem B. 2017 Aug 17;:
Authors: Kashefi M, Thompson LK
Abstract
Bacteria employ remarkable membrane-bound nanoarrays to sense their environment and direct their swimming. Arrays consist of chemotaxis receptor trimers of dimers that are bridged at their membrane-distal tips by rings of two cytoplasmic proteins, a kinase CheA and a...
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08-18-2017 04:59 PM
Stable isotope labeling methods for DNA
Stable isotope labeling methods for DNA
Publication date: Available online 20 June 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Frank H.T. Nelissen, Marco Tessari, Sybren S. Wijmenga, Hans A. Heus</br>
NMR is a powerful method for studying proteins and nucleic acids in solution. The study of nucleic acids by NMR is far more challenging than for proteins, which is mainly due to the limited number of building blocks and unfavorable spectral properties. For NMR studies of DNA molecules, (site specific) isotope enrichment is...
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06-21-2016 01:09 AM
[NMR paper] Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Related Articles Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Angew Chem Int Ed Engl. 2016 May 24;
Authors: Liokatis S, Klingberg R, Tan S, Schwarzer D
Abstract
Post-translational modifications (PTMs) of histones regulate chromatin structure and function. Because nucleosomes contain two copies each of the four core...
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05-25-2016 02:33 PM
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Dynamics and interactions of glycoconjugates probed by stable-isotope-assisted NMR spectroscopy.
Methods Enzymol. 2010;478:305-22
Authors: Yamaguchi Y, Kato K
Unique advantages offered by nuclear magnetic resonance (NMR) spectroscopy provide high-resolution information not only on structures but also on dynamics and interactions of glycoconjugates in solution. These benefits are further enhanced by applying stable-isotope-labeling techniques, which we...
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12-31-2010 07:03 PM
An economical method for producing stable-isotope labeled proteins by the E. coli cel
An economical method for producing stable-isotope labeled proteins by the E. coli cell-free system
Abstract Improvement of the cell-free protein synthesis system (CF) over the past decade have made it one of the most powerful protein production methods. The CF approach is especially useful for stable-isotope (SI) labeling of proteins for NMR analysis. However, it is less popular than expected, partly because the SI-labeled amino acids used for SI labeling by the CF are too expensive. In the present study, we developed a simple and inexpensive method for producing an SI-labeled protein...
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11-07-2010 02:47 PM
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a m
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Related Articles Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Prog Nucl Magn Reson Spectrosc. 2010 May;56(4):346-59
Authors: Kato K, Yamaguchi Y, Arata Y
Illuminating GPCR signaling mechanisms by NMR spectroscopy with stable-isotope labeled receptors
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