Related ArticlesIsotope labeling for studying RNA by solid-state NMR spectroscopy.
J Biomol NMR. 2018 Apr 12;:
Authors: Marchanka A, Kreutz C, Carlomagno T
Abstract
Nucleic acids play key roles in most biological processes, either in isolation or in complex with proteins. Often they are difficult targets for structural studies, due to their dynamic behavior and high molecular weight. Solid-state nuclear magnetic resonance spectroscopy (ssNMR) provides a unique opportunity to study large biomolecules in a non-crystalline state at atomic resolution. Application of ssNMR to RNA, however, is still at an early stage of development and presents considerable challenges due to broad resonances and poor dispersion. Isotope labeling, either as nucleotide-specific, atom-specific or segmental labeling, can resolve resonance overlaps and reduce the line width, thus allowing ssNMR studies of RNA domains as part of large biomolecules or complexes. In this review we discuss the methods for RNA production and purification as well as numerous approaches for isotope labeling of RNA. Furthermore, we give a few examples that emphasize the instrumental role of isotope labeling and ssNMR for studying RNA as part of large ribonucleoprotein complexes.
PMID: 29651587 [PubMed - as supplied by publisher]
Isotope labeling for studying RNA by solid-state NMR spectroscopy
Isotope labeling for studying RNA by solid-state NMR spectroscopy
Abstract
Nucleic acids play key roles in most biological processes, either in isolation or in complex with proteins. Often they are difficult targets for structural studies, due to their dynamic behavior and high molecular weight. Solid-state nuclear magnetic resonance spectroscopy (ssNMR) provides a unique opportunity to study large biomolecules in a non-crystalline state at atomic resolution. Application of ssNMR to RNA, however, is still at an early stage of development and presents...
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04-12-2018 01:11 PM
[NMR paper] Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
J Struct Biol. 2017 Nov 29;:
Authors: Pinto C, Mance D, Julien M, Daniels M, Weingarth M, Baldus M
Abstract
Significant progress has been made in obtaining a structural insight into the assembly of the ?-barrel assembly machinery complex (BAM). These crystallography and electron microscopy studies used detergent as a membrane...
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12-05-2017 07:35 PM
Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules
Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules
Publication date: August 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 96</br>
Author(s): Paul Schanda, Matthias Ernst</br>
Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an overview of experimental approaches to study molecular dynamics by MAS solid-state NMR,...
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04-09-2016 03:54 AM
[NMR paper] Isotope Labeling of Eukaryotic Membrane Proteins in Yeast for Solid-State NMR.
Isotope Labeling of Eukaryotic Membrane Proteins in Yeast for Solid-State NMR.
Related Articles Isotope Labeling of Eukaryotic Membrane Proteins in Yeast for Solid-State NMR.
Methods Enzymol. 2015;565:193-212
Authors: Fan Y, Emami S, Munro R, Ladizhansky V, Brown LS
Abstract
Solid-state NMR (ssNMR) is a rapidly developing technique for exploring structure and dynamics of membrane proteins, but its progress is hampered by its low sensitivity. Despite the latest technological advances, routine ssNMR experiments still require...
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11-19-2015 05:22 PM
[NMR paper] Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png Related Articles Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
PLoS One. 2015;10(4):e0122714
Authors: Wang S, Parthasarathy S, Nishiyama Y, Endo Y, Nemoto T, Yamauchi K, Asakura T,...
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04-11-2015 12:04 AM
[NMR paper] Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR Spectroscopy with Segmental Isotope Labeling.
Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR Spectroscopy with Segmental Isotope Labeling.
Related Articles Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR Spectroscopy with Segmental Isotope Labeling.
Chembiochem. 2014 Nov 12;
Authors: Schubeis T, Lührs T, Ritter C
Abstract
We present an efficient method for the reduction of spectral complexity in the solid-state NMR spectra of insoluble protein assemblies, without loss of signal intensity....
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11-14-2014 08:40 PM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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Proteins
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01-22-2011 03:46 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...
Isotope labeling for studying RNA by solid-state NMR spectroscopy.
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