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Gas-phase unfolding and disassembly reveals stability differences in ligand-bound multiprotein complexes.

Abstract:

Mass spectrometry (MS) is widely used to assess the binding of small molecules to proteins and their complexes. In many cases, subtle differences in the stability afforded by binding of ligands to protein assemblies cannot be detected by MS. Here we show that monitoring the unfolding of protein subunits, using ion mobility-MS, allows differentiation of the effects of ligand binding not normally observed by MS alone. Using wild-type and disease-associated variants of tetrameric transthyretin, ...

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Publication status:
Published

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Journal:
Chemistry and biology More from this journal
Volume:
16
Issue:
4
Pages:
382-390
Publication date:
2009-04-01
DOI:
EISSN:
1879-1301
ISSN:
1074-5521
Language:
English
Keywords:
Pubs id:
pubs:59324
UUID:
uuid:e92b422d-2118-4564-b8dc-2b4be8c021b1
Local pid:
pubs:59324
Source identifiers:
59324
Deposit date:
2012-12-19

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