Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase

Pagel, K.; Natan, E.; Hall, Z.; Fersht, A.R.; Robinson, C.V.— 2013

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.

TitleIntrinsically disordered p53 and its complexes populate compact conformations in the gas phase
AuthorPagel, K.; Natan, E.; Hall, Z.; Fersht, A.R.; Robinson, C.V.
Date2013
Identifier10.1002/anie.201203047
Source(s)
CitationAngew. Chem. Intl. Ed. 2013, 52, 361-365
TypeText