Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions

Research output: Contribution to journal › Journal article › Research › peer-review

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Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions. / Sahin, Cagla; Österlund, Nicklas; Leppert, Axel; Johansson, Jan; Marklund, Erik G.; Benesch, Justin L. P.; Ilag, Leopold L.; Allison, Timothy M.; Landreh, Michael.

In: Chemical Communications, Vol. 57, No. 12, 2021, p. 1450-1453.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Sahin, C, Österlund, N, Leppert, A, Johansson, J, Marklund, EG, Benesch, JLP, Ilag, LL, Allison, TM & Landreh, M 2021, 'Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions', Chemical Communications, vol. 57, no. 12, pp. 1450-1453. https://doi.org/10.1039/d0cc08135c

APA

Sahin, C., Österlund, N., Leppert, A., Johansson, J., Marklund, E. G., Benesch, J. L. P., Ilag, L. L., Allison, T. M., & Landreh, M. (2021). Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions. Chemical Communications, 57(12), 1450-1453. https://doi.org/10.1039/d0cc08135c

Vancouver

Sahin C, Österlund N, Leppert A, Johansson J, Marklund EG, Benesch JLP et al. Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions. Chemical Communications. 2021;57(12):1450-1453. https://doi.org/10.1039/d0cc08135c

Author

Sahin, Cagla ; Österlund, Nicklas ; Leppert, Axel ; Johansson, Jan ; Marklund, Erik G. ; Benesch, Justin L. P. ; Ilag, Leopold L. ; Allison, Timothy M. ; Landreh, Michael. / Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions. In: Chemical Communications. 2021 ; Vol. 57, No. 12. pp. 1450-1453.

Bibtex

@article{fb9a66300b4e491d92bff4a442728087,
title = "Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions",
abstract = "Although native mass spectrometry is widely applied to monitor chemical or thermal protein denaturation, it is not clear to what extent it can inform about alkali-induced unfolding. Here, we probe the relationship between solution- and gas-phase structures of proteins under alkaline conditions. Native ion mobility-mass spectrometry reveals that globular proteins are destabilized rather than globally unfolded, which is supported by solution studies, providing detailed insights into alkali-induced unfolding events. Our results pave the way for new applications of MS to monitor structures and interactions of proteins at high pH.",
author = "Cagla Sahin and Nicklas {\"O}sterlund and Axel Leppert and Jan Johansson and Marklund, {Erik G.} and Benesch, {Justin L. P.} and Ilag, {Leopold L.} and Allison, {Timothy M.} and Michael Landreh",
year = "2021",
doi = "10.1039/d0cc08135c",
language = "English",
volume = "57",
pages = "1450--1453",
journal = "Chemical Communications",
issn = "1359-7345",
publisher = "Royal Society of Chemistry",
number = "12",

}

RIS

TY - JOUR

T1 - Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions

AU - Sahin, Cagla

AU - Österlund, Nicklas

AU - Leppert, Axel

AU - Johansson, Jan

AU - Marklund, Erik G.

AU - Benesch, Justin L. P.

AU - Ilag, Leopold L.

AU - Allison, Timothy M.

AU - Landreh, Michael

PY - 2021

Y1 - 2021

N2 - Although native mass spectrometry is widely applied to monitor chemical or thermal protein denaturation, it is not clear to what extent it can inform about alkali-induced unfolding. Here, we probe the relationship between solution- and gas-phase structures of proteins under alkaline conditions. Native ion mobility-mass spectrometry reveals that globular proteins are destabilized rather than globally unfolded, which is supported by solution studies, providing detailed insights into alkali-induced unfolding events. Our results pave the way for new applications of MS to monitor structures and interactions of proteins at high pH.

AB - Although native mass spectrometry is widely applied to monitor chemical or thermal protein denaturation, it is not clear to what extent it can inform about alkali-induced unfolding. Here, we probe the relationship between solution- and gas-phase structures of proteins under alkaline conditions. Native ion mobility-mass spectrometry reveals that globular proteins are destabilized rather than globally unfolded, which is supported by solution studies, providing detailed insights into alkali-induced unfolding events. Our results pave the way for new applications of MS to monitor structures and interactions of proteins at high pH.

U2 - 10.1039/d0cc08135c

DO - 10.1039/d0cc08135c

M3 - Journal article

C2 - 33439171

AN - SCOPUS:85100866820

VL - 57

SP - 1450

EP - 1453

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 12

ER -

ID: 257658030