2007
DOI: 10.1002/anie.200702161
|View full text |Cite
|
Sign up to set email alerts
|

Ion Mobility–Mass Spectrometry Reveals Long‐Lived, Unfolded Intermediates in the Dissociation of Protein Complexes

Abstract: Recent applications of mass spectrometry (MS) in structural biology have highlighted its ability to define the stoichiometry of numerous protein complexes. [1,2] When combined with tandem MS, this extra dimension has made possible 1) analysis of polydisperse assemblies, [3] 2) characterization of release of proteins from within proteasome and chaperone complexes, [4,5] and 3) identification of proteins released from intact megadalton ribosomes.[6] Tandem MS is effective because macromolecular protein-complex i… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
2

Citation Types

20
223
1

Year Published

2010
2010
2015
2015

Publication Types

Select...
5
3

Relationship

1
7

Authors

Journals

citations
Cited by 220 publications
(244 citation statements)
references
References 28 publications
20
223
1
Order By: Relevance
“…(3) Because unfolding is a time-dependent process, symmetric partitioning is favored when employing surfaceinduced dissociation (a picosecond process [49,50]) instead of CID, which proceeds on a microsecond time scale [30]. (4) Ion mobility measurements on collisionally activated multi-protein complexes confirm the presence of semiunfolded intermediate structures [35,51,52]. (5) Electrostatic models that allow for subunit unfolding yield data that are in qualitative agreement with experimental observations [44].…”
Section: Introductionsupporting
confidence: 61%
See 2 more Smart Citations
“…(3) Because unfolding is a time-dependent process, symmetric partitioning is favored when employing surfaceinduced dissociation (a picosecond process [49,50]) instead of CID, which proceeds on a microsecond time scale [30]. (4) Ion mobility measurements on collisionally activated multi-protein complexes confirm the presence of semiunfolded intermediate structures [35,51,52]. (5) Electrostatic models that allow for subunit unfolding yield data that are in qualitative agreement with experimental observations [44].…”
Section: Introductionsupporting
confidence: 61%
“…Data obtained for Hb suggest that these pre-dissociated states extend to conformations where the departing subunit is almost completely unraveled. Recent molecular dynamics work [75] as well as ion mobility measurements [51] provide further support for the existence of such highly expanded metastable structures.…”
Section: Discussionmentioning
confidence: 91%
See 1 more Smart Citation
“…Instrument development has been integral to these achievements. The work of Robinson et al on the 56 kDa complex of tetrameric transthyretin used IM-MS to examine the activated form of the macromolecular complex [17]. They produced and characterised a number of gasphase structures including tetramer and octamer species as well as a larger range of oligomeric species.…”
Section: Introductionmentioning
confidence: 99%
“…peptides and proteins). [6,7] Because the two methods instrumentally and theoretically match each other, IM-MS can form a two-dimensional (drift time, m/z) spectrum (2D-spectrum). [8][9][10] Like COSY in NMR, [11] it not only provides valuable structural details, but also enables systematical summarization of characterization and practical behavior for the analyte.…”
Section: Introductionmentioning
confidence: 99%