Probing the Conformational Diversity of Cancer-Associated Mutations in p53 with Ion-Mobility Mass Spectrometry


  • This work has been funded by the award of a BBSRC Strategic Industrial Case studentship to E.J. in collaboration with Waters MS technologies.


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Conformational flexibility: The DNA-binding domain of tumor suppressor protein p53 (see picture) is characterized by using ion-mobility mass spectrometry. Wild-type p53 and common single-point carcinogenic mutations exhibit diverse conformational states upon transfer into a solvent-free environment of the mass spectrometer. DNA-binding properties of wild-type p53 and an engineered second-site suppressor mutation H115N were also investigated.