Publication date: 2017 Source:Encyclopedia of Spectroscopy and Spectrometry
Author(s): Bridget A. Becker
Investigating protein–ligand binding using NMR spectroscopy can provide insights into the protein-binding pocket, the contacts the ligand makes with the protein, the bound ligand conformation, and the binding constant. Methods to investigate protein-ligand binding by NMR are divided into two categories: ligand-detected experiments, including diffusion, STD, NOESY, and relaxation experiments, and protein-detected experiments (usually called target-detected experiments), which involve following perturbations of the protein resonance chemical shifts in the presence and absence of ligand. Screening using NMR spectroscopy cannot match in speed and limit of detection screening by high-throughput screening (HTS), but the information content from protein–ligand binding and screening experiments by NMR can be greater, and much weaker binding can be detected. Therein lies the advantage of screening a generally smaller and more tightly focused library of compounds by NMR techniques as compared to HTS screens.
[NMR paper] Labeled Ligand Displacement: Extending NMR-Based Screening of Protein Targets.
Labeled Ligand Displacement: Extending NMR-Based Screening of Protein Targets.
Related Articles Labeled Ligand Displacement: Extending NMR-Based Screening of Protein Targets.
ACS Med Chem Lett. 2010 Sep 9;1(6):295-9
Authors: Swann SL, Song D, Sun C, Hajduk PJ, Petros AM
Abstract
NMR spectroscopy has enjoyed widespread success as a method for screening protein targets, especially in the area of fragment-based drug discovery. However, current methods for NMR-based screening all suffer certain limitations. Two-dimensional methods...
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[NMR paper] (19)F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI).
(19)F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI).
Related Articles (19)F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI).
Org Biomol Chem. 2014 May 6;
Authors: Curtis-Marof R, Doko D, Rowe ML, Richards KL, Williamson RA, Howard MJ
Abstract
We report a protein-observe (19)F NMR-based ligand titration binding study of human PDI b'x with ?-somatostatin that also emphasises...
[NMR paper] G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
Biochem J. 2013 Mar 15;450(3):443-57
Authors: Ding X, Zhao X, Watts A
Abstract
GPCRs (G-protein-coupled receptors) are versatile signalling molecules at the cell surface and make up the largest and most diverse family of membrane receptors in the human genome. They convert a large variety of extracellular stimuli into...
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[NMR paper] NMR spectroscopy techniques for screening and identifying ligand binding to protein r
NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors.
Related Articles NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors.
Angew Chem Int Ed Engl. 2003 Feb 24;42(8):864-90
Authors: Meyer B, Peters T
Binding events of ligands to receptors are the key for an understanding of biological processes. Gaining insight into protein-protein and protein-ligand interactions in solution has recently become possible on an atomic level by new NMR spectroscopic techniques....
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[NMR paper] Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Related Articles Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Biochemistry. 1991 Jun 4;30(22):5524-31
Authors: Gehring K, Williams PG, Pelton JG, Morimoto H, Wemmer DE
Tritium-labeled alpha- and beta-maltodextrins have been used to study their complexes with maltose-binding protein (MBP), a 40-kDa bacterial protein. Five substrates, from maltose to maltohexaose, were labeled at their reducing ends and their binding studied. Tritium NMR spectroscopy...
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[NMR paper] High resolution NMR for screening ligand/protein binding.
High resolution NMR for screening ligand/protein binding.
Related Articles High resolution NMR for screening ligand/protein binding.
Curr Opin Drug Discov Devel. 1999 Jul;2(4):396-400
Authors: Shapiro MJ, Wareing JR
High resolution NMR spectroscopy has provided a versatile tool for assessing ligand/receptor interactions. NMR-based methods are currently being investigated which may prove valuable for compound screening. These techniques include the use of chemical shift perturbations, the monitoring of translational diffusion and the...
Ligand–Protein Binding and Screening Using NMR Spectroscopy
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