Quantifying Labile Protein–Ligand Interactions Using Electrospray Ionization Mass Spectrometry
نویسندگان
چکیده
منابع مشابه
Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry.
A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein-ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand binding. A reference ligand (L(ref)), which binds specifically to the protein (P), at the same bind...
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The application of the direct electrospray ionization mass spectrometry (ESI-MS) assay to quantify interactions between bovine β-lactoglobulin (Lg) and a series of fatty acids (FA), CH(3)(CH(2))(x)COOH, where x=6 (caprylic acid, CpA), 8 (capric acid, CA), 10 (lauric acid, LA), 12 (myristic acid, MA), 14 (palmitic acid, PA) and 16 (stearic acid, SA), is described. Control ESI-MS binding measurem...
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This work investigates the stability of trace (tens of nanograms) deposits of six explosives: erythritol tetranitrate (ETN), pentaerythritol tetranitrate (PETN), cyclotrimethylenetrinitramine (RDX), cyclotetramethylenetetranitramine (HMX), 2,4,6-trinitrotoluene (TNT), and 2,4,6-trinitrophenylmethylnitramine (tetryl) to determine environmental stabilities and lifetimes of trace level materials. ...
متن کاملDesorption electrospray ionization-mass spectrometry of proteins.
Desorption electrospray ionization-mass spectrometry (DESI-MS) was evaluated for the detection of proteins ranging in molecular mass from 12 to 66 kDa. Proteins were uniformly deposited on a solid surface without pretreatment and analyzed with a DESI source coupled to a quadrupole ion trap mass spectrometer. DESI-MS parameters optimized for protein detection included solvent flow rate, temperat...
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ژورنال
عنوان ژورنال: Journal of the American Society for Mass Spectrometry
سال: 2010
ISSN: 1044-0305
DOI: 10.1016/j.jasms.2010.07.008