Six unknown phosphopeptides from p38 and HuR protein kinases discovered
Phosphopeptide identification of protein kinases are a major MS challenge

GC, MDGC

Six unknown phosphopeptides from p38 and HuR protein kinases discovered

08 Jul, 2011

Published over 15 years ago. See the latest and most current information on GC, MDGC.

GC-MS has been used to indentify six unknown phosphopeptides of p38 and HuR protein kinases.

Research published in the Journal of Clinical Bioinformatics showed that further studies are still needed in order to unfold the whole signalling network, which will help towards understanding malignant diseases.

Scientists combined different resins in order to isolate phosphopeptides from p38 and HuR protein kinases in vitro.

Varying phosphopeptides MS strategies were then carried out by the LTQ ion Trap mass spectrometer, while MD bioinformatic simulation was applied to simulate the presence of the extra phosphate group.

The results led to six unknown phosphopeptides of these protein kinases being discovered and amino acid site assignments of the groups from each was validated by inspection of all the spectra.

In addition computer simulation using MD allowed the scientists to produce functional models of the structure and interactions of the phosphorylated kinases.

Recently, GC-MS was used to look into the intesecticidal activity of essential oils in fruits and seeds from the Schinus terebinthifolia Raddi in the fight against malaria and filarial vectors.

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