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

E. Jurneczko, F. Cruickshank, M. Porrini, D.J. Clarke, P.V. Nikolova, I.D.G. Campuzano, M. Morris, P.E. Barran

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)4370-4374
Number of pages5
JournalAngewandte Chemie International Edition
Volume52
Issue number16
DOIs
Publication statusPublished - 15 Apr 2013

Keywords

  • conformation analysis
  • DNA
  • mass spectrometry
  • p53 protein
  • protein structures

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