Premium
Ion Mobility–Mass Spectrometry Reveals Long‐Lived, Unfolded Intermediates in the Dissociation of Protein Complexes
Author(s) -
Ruotolo Brandon T.,
Hyung SukJoon,
Robinson Paula M.,
Giles Kevin,
Bateman Robert H.,
Robinson Carol V.
Publication year - 2007
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.200702161
Subject(s) - dissociation (chemistry) , mass spectrometry , chemistry , ion , ion mobility spectrometry , macromolecule , collision induced dissociation , transthyretin , crystallography , tandem mass spectrometry , chromatography , biochemistry , organic chemistry , biology , endocrinology
Folded or not? Ion mobility–mass spectrometry investigation of an activated macromolecular protein complex lends insight into the structures of intermediates formed in the dissociation process. The activated ions of human tetrameric transthyretin populate partially folded intermediate states (see picture; folded subunits in blue, partially unfolded subunits in red) prior to dissociation.