Abstract
In the absence of crystallographic data, NMR has emerged as the best way to define protein-ligand interactions. Using NMR experiments based on magnetization transfer, one can sort bound from unbound molecules, estimate the dissociation constant, identify contacts implied in the binding, characterize the structure of the bound ligand and conduct ligand competition assays.
Keywords: STD-NMR, WaterLOGSY, epitope mapping, docking, phosphorylated peptide, TrCP complex, binding fragment, protein-ligand interactions, magnetization transfer, dissociation constant, ligand competition assays, ATF4, TrCP, HSQC, MBP, NOESY, ROESY, SCF, TOCSY
Mini-Reviews in Medicinal Chemistry
Title: NMR Applications for Identifying β-TrCP Protein-Ligand Interactions
Volume: 11 Issue: 4
Author(s): J. Pons, V. Tanchou, J.-P. Girault, G. Bertho and N. Evrard-Todeschi
Affiliation:
Keywords: STD-NMR, WaterLOGSY, epitope mapping, docking, phosphorylated peptide, TrCP complex, binding fragment, protein-ligand interactions, magnetization transfer, dissociation constant, ligand competition assays, ATF4, TrCP, HSQC, MBP, NOESY, ROESY, SCF, TOCSY
Abstract: In the absence of crystallographic data, NMR has emerged as the best way to define protein-ligand interactions. Using NMR experiments based on magnetization transfer, one can sort bound from unbound molecules, estimate the dissociation constant, identify contacts implied in the binding, characterize the structure of the bound ligand and conduct ligand competition assays.
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Cite this article as:
Pons J., Tanchou V., Girault J.-P., Bertho G. and Evrard-Todeschi N., NMR Applications for Identifying β-TrCP Protein-Ligand Interactions, Mini-Reviews in Medicinal Chemistry 2011; 11 (4) . https://dx.doi.org/10.2174/138955711795305344
DOI https://dx.doi.org/10.2174/138955711795305344 |
Print ISSN 1389-5575 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5607 |
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