Probing the Conformational Diversity of Cancer‐Associated Mutations in p53 with Ion‐Mobility Mass Spectrometry1. Issue 16 (14th March 2013)

• Record Type: Journal Article
• Authors: Jurneczko, Ewa; Cruickshank, Faye; Porrini, Massimiliano; Clarke, David J.; Campuzano, Iain D. G.; Morris, Michael; Nikolova, Penka V.; Barran, Perdita E.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 16(2013)
• Page Start: 4370
• Page End: 4374
• Publication Date: 2013-03-14
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201210015
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Conformational flexibility</bold>: 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.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1xprfh62" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>