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Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes.

Abstract:
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. (Figure Presented). © 2007 Wiley-VCH Verlag GmbH and Co. KGaA.
Publication status:
Published

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Publisher copy:
10.1002/anie.200702161

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Journal:
Angewandte Chemie (International ed. in English) More from this journal
Volume:
46
Issue:
42
Pages:
8001-8004
Publication date:
2007-01-01
DOI:
EISSN:
1521-3773
ISSN:
1433-7851
Language:
English
Keywords:
Pubs id:
pubs:59305
UUID:
uuid:d2dfe56a-4ee1-41d8-88b9-60b81700a7a4
Local pid:
pubs:59305
Source identifiers:
59305
Deposit date:
2012-12-19

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