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

Abstract

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.