Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase.
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.
Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, UK.
Kevin
K
Pagel
Eviatar
E
Natan
Zoe
Z
Hall
Alan R
AR
Fersht
Carol V
CV
Robinson
D005740:Gases / Q000737:chemistry; D006801:Humans; D013058:Mass Spectrometry; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D017510:Protein Folding; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000378:metabolism
D005740:Gases; D016159:Tumor Suppressor Protein p53