[NMR paper] 2'-(19)F labelling of ribose in RNAs: a tool to analyse RNA/protein interactions by NMR in physiological conditions
2'-(19)F labelling of ribose in RNAs: a tool to analyse RNA/protein interactions by NMR in physiological conditions
Protein-RNA interactions are central to numerous cellular processes. In this work, we present an easy and straightforward NMR-based approach to determine the RNA binding site of RNA binding proteins and to evaluate the binding of pairs of proteins to a single-stranded RNA (ssRNA) under physiological conditions, in this case in nuclear extracts. By incorporation of a ^(19)F atom on the ribose of different nucleotides along the ssRNA sequence, we show that, upon addition of an...
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[NMR paper] Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation
Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation
The study of protein structure, dynamics and function by NMR spectroscopy commonly requires samples that have been enriched ('labelled') with the stable isotopes 13C and/or 15N. The standard approach is to uniformly label a protein with one or both of these nuclei such that all C and/or N sites are in principle 'NMR-visible'. NMR spectra of uniformly labelled proteins can be highly complicated and suffer from signal overlap. Moreover, as molecular size increases...
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[NMR paper] Supramolecular Protein-Polyelectrolyte Assembly at Near Physiological Conditions-Water Proton NMR, ITC, and DLS Study
Supramolecular Protein-Polyelectrolyte Assembly at Near Physiological Conditions-Water Proton NMR, ITC, and DLS Study
The in vivo potency of polyphosphazene immunoadjuvants is inherently linked to the ability of these ionic macromolecules to assemble with antigenic proteins in aqueous solutions and form physiologically stable supramolecular complexes. Therefore, in-depth knowledge of interactions in this biologically relevant system is a prerequisite for a better understanding of mechanism of immunoadjuvant activity. Present study explores a self-assembly of polyphosphazene...
[NMR paper] Structure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR under Nearly Physiological Conditions.
Structure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR under Nearly Physiological Conditions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR under Nearly Physiological Conditions.
J Phys Chem B. 2019 09 12;123(36):7700-7710
Authors: Dingwell DA, Brown LS, Ladizhansky V
Abstract
Human...
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[NMR paper] NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
Related Articles NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
Angew Chem Int Ed Engl. 2013 Sep 20;
Authors: Gil S, Hoek T, Solyom Z, Kümmerle R, Brutscher B, Pierattelli R, Felli IC
Abstract
When approaching physiological conditions, solvent exchange of amide protons in intrinsically disordered proteins (IDPs) is so pronounced that it becomes a key feature to be considered in NMR experiment...
2?-19F labelling of ribose in RNAs: a tool to analyse RNA/protein interactions by NMR in physiological conditions - Frontiers
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