E-mail

E-mail a Wiley Online Library Link

Ewa Jurneczko, Faye Cruickshank, Dr. Massimiliano Porrini, Dr. David J. Clarke, Dr. Iain D. G. Campuzano, Dr. Michael Morris, Dr. Penka V. Nikolova and Dr. Perdita E. Barran Probing the Conformational Diversity of Cancer-Associated Mutations in p53 with Ion-Mobility Mass Spectrometry Angewandte Chemie International Edition 52

Version of Record online: 14 MAR 2013 | DOI: 10.1002/anie.201210015

Thumbnail image of graphical 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.

Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf

Required = Required Field

SEARCH