Calmodulin interaction network investigated by mutational proteomics, chemical cross-linking and mass spectrometry

摘要

We generated a novel CaM-affinity resin with superior specificity as compared to commercial CaM-affinity resin. Our novel CaM-affinity resin combined with site-directed mutagenesis, chemical cross-linking (XL) and tandem mass spectrometry (MS/MS) allowed us to characterize the primary Ca~(2+) -dependent, -independent and -inhibited CaM binding proteomes.