Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase1. Issue 1 (9th July 2012)

• Record Type: Journal Article
• Authors: Pagel, Kevin; Natan, Eviatar; Hall, Zoe; Fersht, Alan R.; Robinson, Carol V.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 1(2013)
• Page Start: 361
• Page End: 365
• Publication Date: 2012-07-09
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201203047
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Spontaneous shrinking</bold>: The intrinsically disordered tumor suppressor protein p53 was analyzed by using a combination of ion mobility mass spectrometry and molecular dynamics simulations. Structured p53 subdomains retain their overall topology upon transfer into the gas phase. When intrinsically disordered segments are introduced into the protein sequence, however, the complex spontaneously collapses in the gas phase to a compact conformation.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1pjrq1p3" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>