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Charge engineering reveals the roles of ionizable side chains in electrospray ionization mass spectrometry

Abstract:

In solution, the charge of a protein is intricately linked to its stability, but electrospray ionization distorts this connection, potentially limiting the ability of native mass spectrometry to inform about protein structure and dynamics. How the behavior of intact proteins in the gas phase depends on the presence and distribution of ionizable surface residues has been difficult to answer because multiple chargeable sites are present in virtually all proteins. Turning to protein engineering,...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/jacsau.1c00458

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Role:
Author
ORCID:
0000-0002-6048-6896
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Publisher:
American Chemical Society Publisher's website
Journal:
JACS Au Journal website
Volume:
1
Issue:
12
Pages:
2385–2393
Publication date:
2021-11-29
Acceptance date:
2021-11-13
DOI:
EISSN:
2691-3704
Language:
English
Keywords:
Pubs id:
1213035
Local pid:
pubs:1213035
Deposit date:
2021-12-01

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