False-positive rate determination of protein target discovery using a covalent modification- and mass spectrometry-based proteomics platform.

ABSTRACT: Detection and quantitation of protein-ligand binding interactions is important in many areas of biological research. Stability of proteins from rates of oxidation (SPROX) is an energetics-based technique for identifying the proteins targets of ligands in complex biological mixtures. Knowing the false-positive rate of protein target discovery in proteome-wide SPROX experiments is important for the correct interpretation of results. Reported here are the results of a control SPROX experiment in which chemical denaturation data is obtained on the proteins in two samples that originated from the same yeast lysate, as would be done in a typical SPROX experiment except that one sample would be spiked with the test ligand. False-positive rates of 1.2-2.2% and <0.8% are calculated for SPROX experi

SUBMITTER: Strickland EC 

PROVIDER: S-EPMC3880622 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature