Saturation transfer difference spectroscopy

From NMR Wiki

Saturation transfer difference (STD) spectroscopy allows to detect transient binding of small molecule ligands to macromolecular receptors. Receptor species include proteins - free in solution or immobilized, whole virus particles, etc.

Range of applicable dissociation constants is approximately 10^-3-10^-8 M.

STD method can be used to determine epitope of ligand binding, since most strongly interacting groups of ligand will show stronger STD effect.

References

1. Meyer, B and Peters, T. NMR Spectroscopy Techniques for Screening and Identifying Ligand Binding to Protein Receptors. Angewandte Chemie International Edition 42(8):864--890, 2003. BibTeX [meyer03]

2. MAYER, M and MEYER, B. CHARACTERIZATION OF LIGAND BINDING BY SATURATION TRANSFER DIFFERENCE NMR SPECTROSCOPY. Angewandte Chemie(International ed Print) 38(12):1784--1788, 1999. BibTeX [meyer99]

3. Streiff, JH and Juranic, NO and Macura, SI and Warner, DO and Jones, KA and Perkins, WJ. Saturation transfer difference nuclear magnetic resonance spectroscopy as a method for screening proteins for anesthetic binding. Mol Pharmacol 66:929--935, 2004. BibTeX [stre04]

4. Mayer, M and Meyer, B. Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J Am Chem Soc 123(25):6108--17, 2001. BibTeX [mayer01]