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Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase
Author(s) -
Pagel Kevin,
Natan Eviatar,
Hall Zoe,
Fersht Alan R.,
Robinson Carol V.
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.201203047
Subject(s) - gas phase , computer science , intrinsically disordered proteins , phase (matter) , sequence (biology) , chemical physics , service (business) , topology (electrical circuits) , physics , nanotechnology , chemistry , materials science , thermodynamics , quantum mechanics , engineering , electrical engineering , biochemistry , economy , economics , nuclear magnetic resonance
Spontaneous shrinking : 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.