Cytoskeletal microtubule-associated Proteins (MAPs) are proteins important for regulating the stability and dynamics of the microtubule. Phosphorylation of MAP2c and Tau regulates their binding to the microtubules and to different proteins important for neurons plasticity. We have previously expressed glycogen synthase kinase (GSK3) in our lab, and recorded the phosphorylation of MAP2c by NMR, revealing more than 10 phosphorylation sites on MAP2c. Possible phosphorylation sites were determined by mass spectrometry, but only one phosphorylation site could be assigned in NMR spectra. The task of the student would be to express mutants of MAP2c where possible phosphorylation sites have been deleted, to purify the protein, to follow phosphorylation of the mutant by NMR, to assign observed signals to phosphorylated residues, and to compare the results with data described in the literature. The result should contribute to understanding specificity in regulation of MAP activity.