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

Abstract

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.

DOI: 10.1002/anie.201203047
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@article{Pagel2013IntrinsicallyDP, title={Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase.}, author={Kevin Pagel and Eviatar Natan and Zoe Hall and Alan R. Fersht and Carol V Robinson}, journal={Angewandte Chemie}, year={2013}, volume={52 1}, pages={361-5} }