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 RNA binding protein,...
[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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11-17-2022 11:19 AM
[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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08-13-2020 10:14 PM
Nitrogen-detected TROSY yields comparable sensitivity to proton-detected TROSY for non-deuterated, large proteins under physiological salt conditions
Nitrogen-detected TROSY yields comparable sensitivity to proton-detected TROSY for non-deuterated, large proteins under physiological salt conditions
Abstract
Direct detection of the TROSY component of proton-attached 15N nuclei (15N-detected TROSY) yields high quality spectra with high field magnets, by taking advantage of the slow 15N transverse relaxation. The slow transverse relaxation and narrow line width of the 15N-detected TROSY resonances are expected to compensate for the inherently low 15N sensitivity. However, the sensitivity of...
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01-23-2016 03:35 PM
[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, Hošek 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...
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10-12-2013 05:24 PM
The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.
The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.
The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.
Biochem Biophys Res Commun. 2010 Nov 26;402(4):705-10
Authors: Huang HW, Mohan SK, Yu C
Human epidermal growth factor (hEGF) induces the proliferation, differentiation and survival of various cell types including tumor-derived cells. Generally, hEGF performs its biological function by binding to a specific...
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01-14-2011 12:05 PM
[NMR paper] Spin labels as a tool to identify and characterize protein-ligand interactions by NMR
Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy.
Related Articles Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy.
Chembiochem. 2002 Mar 1;3(2-3):167-73
Authors: Jahnke W
NMR spectroscopy based discovery and optimization of lead compounds for a given molecular target requires the development of methods with maximum sensitivity and robustness. It is shown here that organic nitroxide radicals ("spin labels") can be used to boost the sensitivity...
2'-(19)F labelling of ribose in RNAs: a tool to analyse RNA/protein interactions by NMR in physiological conditions
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