Site-Specific Kinetic Analysis of Wildtype Sic1 Phosphorylation by Liquid Chromatography Fourier Transform-Ion Cyclotron Resonance Mass Spectrometry

摘要

From a bottom-up approach, the site-specific phosphorylation kinetics can be measured for mathematical models of the Sic1 switch-like behavior. It appears that each of the six quantified sites have a different phosphorylation rate. According to previously published data, the sites that most significantly contribute to Sic1 degradation are T45, S76, T5, and T33. We have not yet measured T5 kinetics, however, the 33-50 and 54-79 peptides have higher rates of phosphorylation than the 80-84 and 186-193 peptides, so our data correlate well with previouswork. Future work includes completing kinetic studies by quantifying the remaining peptides as well as making comparisons to mathematical models created by our coauthors.