Use of selected reaction monitoring data for label-free quantification of protein modification stoichiometry.
Quantification of protein and PTM abundance in biological samples is an important component of proteomic studies. Label-free methods for quantification using MS are attractive because they are simple to implement and applicable to any experimental system. We demonstrate that PTM stoichiometry can be accurately measured using label-free quantification and selected reaction monitoring. Use of selected reaction monitoring is advantageous with complex biological samples and we show this approach can be used to quantify multiple PTMs independently on a single peptide.
Department of Biological Sciences, Purdue University, West Lafayette, IN, USA.
Deepa
D
Balasubramaniam
Christie L
CL
Eissler
Cynthia V
CV
Stauffacher
Mark C
MC
Hall
D000595:Amino Acid Sequence; D002457:Cell Extracts; D005656:Fungal Proteins / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010748:Phosphopeptides / Q000737:chemistry*; D010766:Phosphorylation; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics / Q000379:methods; D036104:Receptor, EphA2 / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry
D002457:Cell Extracts; D005656:Fungal Proteins; D010446:Peptide Fragments; D010748:Phosphopeptides; D011506:Proteins; D011994:Recombinant Proteins; D036104:Receptor, EphA2