+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Saturation transfer difference nuclear magnetic resonance spectroscopy as a method for screening proteins for anesthetic binding



Saturation transfer difference nuclear magnetic resonance spectroscopy as a method for screening proteins for anesthetic binding



Molecular Pharmacology 66(4): 929-935



The effects of anesthetics on cellular function may result from direct interactions between anesthetic molecules and proteins. These interactions have a low affinity and are difficult to characterize. To identify proteins that bind anesthetics, we used nuclear magnetic resonance saturation transfer difference (STD) spectroscopy. The method is based on the nuclear Overhauser effect between bound anesthetic protons and all protein protons. To establish STD as a method for testing anesthetic binding to proteins, we conducted measurements on a series of protein/anesthetic solutions studied before by other methods. STD was able to identify that volatile anesthetics bind to bovine serum albumin, oleic acid reduces halothane binding to bovine serum albumin, and halothane binds to apomyoglobin but not lysozyme. Using STD, we found that halothane binding to calmodulin is Ca2+ -dependent, which demonstrates anesthetic specificity for a protein conformation. Thus, STD is a powerful tool for investigating anesthetic-protein interactions because of its abilities to detect weak binding, to screen a single protein for binding of multiple anesthetics simultaneously, and to detect a change in anesthetic binding caused by conformational changes or competition with other ligands.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 012534801

Download citation: RISBibTeXText

PMID: 15385643


Related references

Interaction between Wine Phenolic Acids and Salivary Proteins by Saturation-Transfer Difference Nuclear Magnetic Resonance Spectroscopy (STD-NMR) and Molecular Dynamics Simulations. Journal of Agricultural and Food Chemistry 65(31): 6434-6441, 2017

Recent developments and applications of saturation transfer difference nuclear magnetic resonance (STD NMR) spectroscopy. Molecular Biosystems 9(4): 571-577, 2013

Saturation transfer difference nuclear magnetic resonance study on the specific binding of ligand to protein. Analytical Biochemistry 385(2): 380-382, 2009

Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistep-binding of l-fucose to norovirus particles. Glycobiology 27(1): 80-86, 2017

Understanding solution-state noncovalent interactions between xenobiotics and natural organic matter using 19F/1H heteronuclear saturation transfer difference nuclear magnetic resonance spectroscopy. Environmental Toxicology and Chemistry 30(8): 1745-1753, 2011

Investigation of the binding and cleavage characteristics of N1 neuraminidases from avian, seasonal, and pandemic influenza viruses using saturation transfer difference nuclear magnetic resonance. Influenza and other Respiratory Viruses 8(2): 235-242, 2014

Use of NMR saturation transfer difference spectroscopy to study ligand binding to membrane proteins. Methods in Molecular Biology 914: 47-63, 2012

Dynamic aspects of antibody:oligosaccharide complexes characterized by molecular dynamics simulations and saturation transfer difference nuclear magnetic resonance. Glycobiology 21(12): 1570-1579, 2011

Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly higher affinity of integrin alpha(IIb)beta3 in native platelets than in liposomes. Journal of the American Chemical Society 127(3): 916-919, 2005

Determination of mitochondrial creatine kinase fluxes in intact heart mitochondria using 31P-saturation transfer nuclear magnetic resonance spectroscopy. Biochimica Et Biophysica Acta. 1365(3): 503-512, Y 20, 1998

Nuclear magnetic resonance studies of amino acids and proteins. Rotational correlation times of proteins by deuterium nuclear magnetic resonance spectroscopy. Biochemistry 22(12): 2908-2913, 1983

Proton nuclear magnetic resonance saturation transfer studies of coenzyme binding to Lactobacillus casei dihydrofolate reductase. Biochemistry 19(16): 3738-3746, 1980

Multidimensional nuclear magnetic resonance spectroscopy of DNA-binding proteins. Methods in Enzymology 208: 63-82, 1991

Nuclear magnetic resonance studies of carbonic anhydrase catalyzed reversible hydration of acetaldehyde by the saturation transfer method. Biochemistry 19(9): 1866-1873, 1980

Measurement of rapid membrane exchange by saturation transfer nuclear magnetic resonance spectroscopy Permeability of the erythrocyte membrane to NH-4 + NH-8. Blood 82(10 Suppl. 1): 7A, 1993