Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry

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Standard

Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry. / Abramsson, Mia L.; Sahin, Cagla; Hopper, Jonathan T. S.; Branca, Rui M. M.; Danielsson, Jens; Xu, Mingming; Chandler, Shane A.; Österlund, Nicklas; Ilag, Leopold L.; Leppert, Axel; Costeira-Paulo, Joana; Lang, Lisa; Teilum, Kaare; Laganowsky, Arthur; Benesch, Justin L. P.; Oliveberg, Mikael; Robinson, Carol V.; Marklund, Erik G.; Allison, Timothy M.; Winther, Jakob R.; Landreh, Michael.

I: JACS Au, Bind 1, Nr. 12, 2021, s. 2385-2393.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Abramsson, ML, Sahin, C, Hopper, JTS, Branca, RMM, Danielsson, J, Xu, M, Chandler, SA, Österlund, N, Ilag, LL, Leppert, A, Costeira-Paulo, J, Lang, L, Teilum, K, Laganowsky, A, Benesch, JLP, Oliveberg, M, Robinson, CV, Marklund, EG, Allison, TM, Winther, JR & Landreh, M 2021, 'Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry', JACS Au, bind 1, nr. 12, s. 2385-2393. https://doi.org/10.1021/jacsau.1c00458

APA

Abramsson, M. L., Sahin, C., Hopper, J. T. S., Branca, R. M. M., Danielsson, J., Xu, M., Chandler, S. A., Österlund, N., Ilag, L. L., Leppert, A., Costeira-Paulo, J., Lang, L., Teilum, K., Laganowsky, A., Benesch, J. L. P., Oliveberg, M., Robinson, C. V., Marklund, E. G., Allison, T. M., ... Landreh, M. (2021). Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry. JACS Au, 1(12), 2385-2393. https://doi.org/10.1021/jacsau.1c00458

Vancouver

Abramsson ML, Sahin C, Hopper JTS, Branca RMM, Danielsson J, Xu M o.a. Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry. JACS Au. 2021;1(12):2385-2393. https://doi.org/10.1021/jacsau.1c00458

Author

Abramsson, Mia L. ; Sahin, Cagla ; Hopper, Jonathan T. S. ; Branca, Rui M. M. ; Danielsson, Jens ; Xu, Mingming ; Chandler, Shane A. ; Österlund, Nicklas ; Ilag, Leopold L. ; Leppert, Axel ; Costeira-Paulo, Joana ; Lang, Lisa ; Teilum, Kaare ; Laganowsky, Arthur ; Benesch, Justin L. P. ; Oliveberg, Mikael ; Robinson, Carol V. ; Marklund, Erik G. ; Allison, Timothy M. ; Winther, Jakob R. ; Landreh, Michael. / Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry. I: JACS Au. 2021 ; Bind 1, Nr. 12. s. 2385-2393.

Bibtex

@article{8b57c5ed38db486f83f62303d85518dd,

title = "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, we show that ionizable side chains are completely dispensable for charging under native conditions, but if present, they are preferential protonation sites. The absence of ionizable side chains results in identical charge state distributions under native-like and denaturing conditions, while coexisting conformers can be distinguished using ion mobility separation. An excess of ionizable side chains, on the other hand, effectively modulates protein ion stability. In fact, moving a single ionizable group can dramatically alter the gas-phase conformation of a protein ion. We conclude that although the sum of the charges is governed solely by Coulombic terms, their locations affect the stability of the protein in the gas phase.",

author = "Abramsson, {Mia L.} and Cagla Sahin and Hopper, {Jonathan T. S.} and Branca, {Rui M. M.} and Jens Danielsson and Mingming Xu and Chandler, {Shane A.} and Nicklas {\"O}sterlund and Ilag, {Leopold L.} and Axel Leppert and Joana Costeira-Paulo and Lisa Lang and Kaare Teilum and Arthur Laganowsky and Benesch, {Justin L. P.} and Mikael Oliveberg and Robinson, {Carol V.} and Marklund, {Erik G.} and Allison, {Timothy M.} and Winther, {Jakob R.} and Michael Landreh",

note = "{\textcopyright} 2021 The Authors. Published by American Chemical Society.",

year = "2021",

doi = "10.1021/jacsau.1c00458",

language = "English",

volume = "1",

pages = "2385--2393",

journal = "JACS Au",

issn = "2691-3704",

publisher = "American Chemical Society",

number = "12",

}

RIS

TY - JOUR

T1 - Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry

AU - Abramsson, Mia L.

AU - Sahin, Cagla

AU - Hopper, Jonathan T. S.

AU - Branca, Rui M. M.

AU - Danielsson, Jens

AU - Xu, Mingming

AU - Chandler, Shane A.

AU - Österlund, Nicklas

AU - Ilag, Leopold L.

AU - Leppert, Axel

AU - Costeira-Paulo, Joana

AU - Lang, Lisa

AU - Teilum, Kaare

AU - Laganowsky, Arthur

AU - Benesch, Justin L. P.

AU - Oliveberg, Mikael

AU - Robinson, Carol V.

AU - Marklund, Erik G.

AU - Allison, Timothy M.

AU - Winther, Jakob R.

AU - Landreh, Michael

PY - 2021

Y1 - 2021

N2 - 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, we show that ionizable side chains are completely dispensable for charging under native conditions, but if present, they are preferential protonation sites. The absence of ionizable side chains results in identical charge state distributions under native-like and denaturing conditions, while coexisting conformers can be distinguished using ion mobility separation. An excess of ionizable side chains, on the other hand, effectively modulates protein ion stability. In fact, moving a single ionizable group can dramatically alter the gas-phase conformation of a protein ion. We conclude that although the sum of the charges is governed solely by Coulombic terms, their locations affect the stability of the protein in the gas phase.

AB - 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, we show that ionizable side chains are completely dispensable for charging under native conditions, but if present, they are preferential protonation sites. The absence of ionizable side chains results in identical charge state distributions under native-like and denaturing conditions, while coexisting conformers can be distinguished using ion mobility separation. An excess of ionizable side chains, on the other hand, effectively modulates protein ion stability. In fact, moving a single ionizable group can dramatically alter the gas-phase conformation of a protein ion. We conclude that although the sum of the charges is governed solely by Coulombic terms, their locations affect the stability of the protein in the gas phase.

U2 - 10.1021/jacsau.1c00458

DO - 10.1021/jacsau.1c00458

M3 - Journal article

C2 - 34977906

VL - 1

SP - 2385

EP - 2393

JO - JACS Au

JF - JACS Au

SN - 2691-3704

IS - 12

ER -

ID: 289963521

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