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Probing the Conformational Diversity of Cancer‐Associated Mutations in p53 with Ion‐Mobility Mass Spectrometry
Author(s) -
Jurneczko Ewa,
Cruickshank Faye,
Porrini Massimiliano,
Clarke David J.,
Campuzano Iain D. G.,
Morris Michael,
Nikolova Penka V.,
Barran Perdita E.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201210015
Subject(s) - mass spectrometry , chemistry , point mutation , suppressor , dna , p53 protein , ion mobility spectrometry , wild type , biophysics , mutant , mutation , biochemistry , biology , chromatography , gene
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.