Journal of Undergraduate Research
Keywords
phosphoester bond stabilization, enhanced CID phosphoproteomics
College
Physical and Mathematical Sciences
Department
Chemistry and Biochemistry
Abstract
Proteomics uses highly sensitive mass spectrometers to measure peptide fragment masses from enzymatically digested proteins. Measuring the mass of the peptide and fragments produced in the mass spectrometer allows for identification of its parent protein. Phosphoproteomics analyzes peptides that have been phosphorylated. Phosphoproteomics identifies phosphorylation sites, network relationships between proteins, and how cells respond to changes in their environment. Mass spectrometers typically ionize peptides to carry positive charges. This charge aids to draw molecules into the instrument. Phosphate modifications reduce charge on their molecules, reducing the positive charge on phosphopeptides, creating neutral, or negatively charged species. The lack of charge on these species results in a loss of detection.1-2
Recommended Citation
Morley, Stewart and Prince, Dr. John
(2013)
"Phosphoester Bond Stabilization for Enhanced CID Phosphoproteomics,"
Journal of Undergraduate Research: Vol. 2013:
Iss.
1, Article 2575.
Available at:
https://scholarsarchive.byu.edu/jur/vol2013/iss1/2575