Related Experiment Video
Updated: May 22, 2025

Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF
Published on: January 12, 2024
The Hunt Lab Weighs in on Mass Spectrometry-Based Analysis of Protein Posttranslational Modifications
Joshua J Coon1, Jarrod A Marto2, John E P Syka3
1Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA; Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA; Morgridge Institute for Research, Madison, Wisconsin, USA.
Researchers developed new methods for identifying protein modifications. Electron transfer dissociation improves analysis of phosphorylation and other labile modifications, advancing phosphoproteomics.
Area of Science:
- Biochemistry
- Proteomics
- Mass Spectrometry
Background:
- Identifying protein posttranslational modifications is difficult due to low abundance and dynamic regulation.
- Early phosphopeptide enrichment methods enabled large-scale analysis of protein phosphorylation (phosphoproteomics).
More Related Videos
11:02Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
Published on: May 17, 2016
17:12Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS
Published on: December 20, 2010
Related Concept Videos
MALDI-TOF Mass Spectrometry
Matrix-assisted laser desorption ionization (MALDI) is a commonly...
Proteomics
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...