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Mass spectrometry reveals the direct action of a chemical chaperone

Abstract:

Despite their fundamental biological importance and therapeutic potential, the interactions between chemical chaperones and proteins remain difficult to capture due to their transient and nonspecific nature. Using a simple mass spectrometric assay, we are able to follow the interactions between proteins and the chemical chaperone trimethylamine-N-oxide (TMAO). In this manner, we directly observe that the counteraction of TMAO and the denaturant urea is driven by the exclusion of TMAO from the...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's Version

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Publisher copy:
10.1021/acs.jpclett.8b01817

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry; Physical & Theoretical Chem
ORCID:
0000-0001-7686-2983
Lianoudaki, D More by this author
Kaldmäe, M More by this author
Kronqvist, N More by this author
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Publisher:
American Chemical Society Publisher's website
Journal:
The Journal of Physical Chemistry Letters Journal website
Volume:
9
Issue:
14
Pages:
4082-4086
Publication date:
2018-07-05
Acceptance date:
2018-07-05
DOI:
EISSN:
1948-7185
Pubs id:
pubs:869322
URN:
uri:976886ed-7f30-4d41-baf4-d7af8d724d42
UUID:
uuid:976886ed-7f30-4d41-baf4-d7af8d724d42
Local pid:
pubs:869322
Language:
English
Keywords:

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