Related Experiment Video
Updated: Jun 4, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Tyrosine Phosphorylation Site Identification by MALDI-MS
Abstract:
INTRODUCTIONIn this protocol, radiolabeled proteins are separated using SDS-PAGE and digested in-gel. The phosphopeptides are subjected to two-dimensional LC and identified by MALDI-MS and MALDI-PSD. The identification of eight tyrosine phosphorylation sites in the human Gab-1 protein is provided as an example of the method's utility. The expression and phosphorylation of human Gab-1 with the insulin receptor kinase in vitro are summarized as an example of this approach to identifying phosphorylated tyrosine residues.
More Related Videos
Related Concept Videos
Peptide Identification Using Tandem Mass Spectrometry
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
MALDI-TOF Mass Spectrometry
Rapid Identification of Pathogens
Matrix-Assisted Laser Desorption Ionization (MALDI)

