title: Analysis of the Global Changes in SH2 Binding Properties Using Mass Spectrometry Supported by Quantitative Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) Technique.
abstract: Quantitative mass spectrometry (MS)-based proteomics enables fast and reliable analysis of protein complexes. Its robustness and sensitivity effectively substitute traditional antibody-based approaches. Here, we describe the combination of mass spectrometry and Stable Isotope Labeling by Amino acids in Cell culture (SILAC) in characterization of the SH2 domain binding capacity.
authors.affiliation: Systems Structural Biology Group, Institute of Molecular and Cell Biology (IMCB), Agency for Science, Technology and Research (A*STAR), Singapore, Singapore. rmsobota@imcb.a-star.edu.sg.
authors.forename: Radoslaw M
authors.initials: RM
authors.lastname: Sobota
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D018929:Cell Culture Techniques; D006367:HeLa Cells; D006801:Humans; D007553:Isotope Labeling / Q000379:methods; D013058:Mass Spectrometry / Q000379:methods; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D040901:Proteomics / Q000379:methods; D011993:Recombinant Fusion Proteins; D057188:Workflow; D018909:src Homology Domains
chemical_list: D000596:Amino Acids; D010455:Peptides; D011506:Proteins; D011993:Recombinant Fusion Proteins
keywords: Peptide pull down; Quantitative mass spectrometry; SH2 domains; SILAC