Journal article
Charge engineering reveals the roles of ionizable side chains in electrospray ionization mass spectrometry
- Abstract:
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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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(Version of record, 2.9MB)
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- Publisher copy:
- 10.1021/jacsau.1c00458
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Authors
Funding
Bibliographic Details
- 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
Item Description
- Language:
- English
- Keywords:
- Pubs id:
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1213035
- Local pid:
- pubs:1213035
- Deposit date:
- 2021-12-01
Terms of use
- Copyright holder:
- Abramsson et al.
- Copyright date:
- 2021
- Rights statement:
- ©2021 The Authors. Published by American Chemical Society. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
- Licence:
- CC Attribution (CC BY)
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