Abstract
Protein-observed (19)F (PrOF) NMR is an emerging tool for ligand discovery. To optimize the efficiency of PrOF NMR experiments, paramagnetic relaxation enhancement through the addition of chelated Ni(II) was used to shorten longitudinal relaxation time without causing significant line broadening. Thus enhancing relaxation time leads to shorter experiments without perturbing the binding of low- or high-affinity ligands. This method allows for time-efficient screening of potential ligands for a wide variety of proteins in the growing field of fragment-based ligand discovery.
[NMR paper] Fast and Efficient Fragment-Based Lead Generation by Fully Automated Processing and Analysis of Ligand-Observed NMR Binding Data.
Fast and Efficient Fragment-Based Lead Generation by Fully Automated Processing and Analysis of Ligand-Observed NMR Binding Data.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Fast and Efficient Fragment-Based Lead Generation by Fully Automated Processing and Analysis of Ligand-Observed NMR Binding Data.
J Med Chem. 2016 Apr 14;59(7):3303-10
Authors: Peng C, Frommlet A, Perez M, Cobas C, Blechschmidt A, Dominguez S, Lingel A
Abstract
NMR...
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[NMR paper] Protein-observed (19)F-NMR for fragment screening, affinity quantification and druggability assessment.
Protein-observed (19)F-NMR for fragment screening, affinity quantification and druggability assessment.
Protein-observed (19)F-NMR for fragment screening, affinity quantification and druggability assessment.
Nat Protoc. 2016 Aug;11(8):1414-27
Authors: Gee CT, Arntson KE, Urick AK, Mishra NK, Hawk LM, Wisniewski AJ, Pomerantz WC
Abstract
NMR spectroscopy can be used to quantify the binding affinity between proteins and low-complexity molecules, termed 'fragments'; this versatile screening approach allows researchers to assess the...
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[NMR paper] Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.
Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.
Related Articles Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.
J Biomol NMR. 2016 Jan 4;
Authors: Tamaki H, Egawa A, Kido K, Kameda T, Kamiya M, Kikukawa T, Aizawa T, Fujiwara T, Demura M
Abstract
Magic angle spinning...
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Structure determination of uniformly 13 C, 15 N labeled protein using qualitative distance restraints from MAS solid-state 13 C-NMR observed paramagnetic relaxation enhancement
Structure determination of uniformly 13 C, 15 N labeled protein using qualitative distance restraints from MAS solid-state 13 C-NMR observed paramagnetic relaxation enhancement
Abstract
Magic angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) is a powerful method for structure determination of insoluble biomolecules. However, structure determination by MAS solid-state NMR remains challenging because it is difficult to obtain a sufficient amount of distance restraints owing to spectral complexity. Collection of distance restraints from...
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[NMR paper] Fragment Screening and Druggability Assessment for the CBP/p300 KIX Domain through Protein-Observed (19) F NMR Spectroscopy.
Fragment Screening and Druggability Assessment for the CBP/p300 KIX Domain through Protein-Observed (19) F NMR Spectroscopy.
Fragment Screening and Druggability Assessment for the CBP/p300 KIX Domain through Protein-Observed (19) F NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Feb 4;
Authors: Gee CT, Koleski EJ, Pomerantz WC
Abstract
(19) F NMR spectroscopy of labeled proteins is a sensitive method for characterizing structure, conformational dynamics, higher-order assembly, and ligand binding. Fluorination of aromatic side...
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Requirements on Paramagnetic Relaxation Enhancement Data for Membrane Protein Structure Determination by NMR
Requirements on Paramagnetic Relaxation Enhancement Data for Membrane Protein Structure Determination by NMR
6 June 2012
Publication year: 2012
Source:Structure, Volume 20, Issue 6</br>
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Nuclear magnetic resonance (NMR) structure calculations of the ?-helical integral membrane proteins DsbB, GlpG, and halorhodopsin show that distance restraints from paramagnetic relaxation enhancement (PRE) can provide sufficient structural information to determine their structure with an accuracy of about 1.5*Å in the absence of other long-range conformational restraints. Our...
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Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
J Phys Chem Lett. 2011 Jul 21;2(14):1836-1841
Authors: Tang M, Berthold DA, Rienstra CM
Membrane proteins play an important role in many biological functions. Solid-state NMR spectroscopy is uniquely suited for studying structure and dynamics of membrane proteins in a membranous environment. The major challenge to obtain high quality solid-state NMR spectra of membrane proteins is...
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[Question from NMRWiki Q&A forum] Relaxation editing vr paramagnetic relaxation enhancement experiments - 13C CP-MAS NM
Relaxation editing vr paramagnetic relaxation enhancement experiments - 13C CP-MAS NMR
I am a beginner in NMR spectroscopy and I would like to learn more about relaxation editing experiments vs PRE. A colleague of mine is doing the 13C CP-MAS NMR experim. and he using cellulose II powder, regenerated cellulose and milled reg cellulose. We are interested in C4 resonance of cellulose II, good resolved resonance, to better understand the supramolecular structure of cellulose II. As experiments: long relaxation experiments - PRE with aqueous CuSO4 solution of certain concentration, does the...
Paramagnetic relaxation enhancement for protein-observed (19)F NMR as an enabling approach for efficient fragment screening.
Linear Mode
