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Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons32738

Pagel,  Kevin
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford;

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Pagel, K., Natan, E., Hall, Z., Fersht, A. R., & Robinson, C. V. (2013). Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase. Angewandte Chemie: eine Zeitschrift der Gesellschaft Deutscher Chemiker, 125(1), 379-383. doi:10.1002/ange.201203047.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-735E-9
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.