Advances in mass spectrometry to unravel the structure and function of protein condensates

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Advances in mass spectrometry to unravel the structure and function of protein condensates. / Sahin, Cagla; Leppert, Axel; Landreh, Michael.

In: Nature Protocols, Vol. 18, 2023, p. 3653–3661.

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

Harvard

Sahin, C, Leppert, A & Landreh, M 2023, 'Advances in mass spectrometry to unravel the structure and function of protein condensates', Nature Protocols, vol. 18, pp. 3653–3661. https://doi.org/10.1038/s41596-023-00900-0

APA

Sahin, C., Leppert, A., & Landreh, M. (2023). Advances in mass spectrometry to unravel the structure and function of protein condensates. Nature Protocols, 18, 3653–3661. https://doi.org/10.1038/s41596-023-00900-0

Vancouver

Sahin C, Leppert A, Landreh M. Advances in mass spectrometry to unravel the structure and function of protein condensates. Nature Protocols. 2023;18:3653–3661. https://doi.org/10.1038/s41596-023-00900-0

Author

Sahin, Cagla ; Leppert, Axel ; Landreh, Michael. / Advances in mass spectrometry to unravel the structure and function of protein condensates. In: Nature Protocols. 2023 ; Vol. 18. pp. 3653–3661.

Bibtex

@article{9e40a6f1b2b44d1aa28677bbb89d8ca1,
title = "Advances in mass spectrometry to unravel the structure and function of protein condensates",
abstract = "Membrane-less organelles assemble through liquid–liquid phase separation (LLPS) of partially disordered proteins into highly specialized microenvironments. Currently, it is challenging to obtain a clear understanding of the relationship between the structure and function of phase-separated protein assemblies, owing to their size, dynamics and heterogeneity. In this Perspective, we discuss recent advances in mass spectrometry (MS) that offer several promising approaches for the study of protein LLPS. We survey MS tools that have provided valuable insights into other insoluble protein systems, such as amyloids, and describe how they can also be applied to study proteins that undergo LLPS. On the basis of these recent advances, we propose to integrate MS into the experimental workflow for LLPS studies. We identify specific challenges and future opportunities for the analysis of protein condensate structure and function by MS.",
author = "Cagla Sahin and Axel Leppert and Michael Landreh",
note = "Publisher Copyright: {\textcopyright} 2023, Springer Nature Limited.",
year = "2023",
doi = "10.1038/s41596-023-00900-0",
language = "English",
volume = "18",
pages = "3653–3661",
journal = "Nature Protocols",
issn = "1754-2189",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Advances in mass spectrometry to unravel the structure and function of protein condensates

AU - Sahin, Cagla

AU - Leppert, Axel

AU - Landreh, Michael

N1 - Publisher Copyright: © 2023, Springer Nature Limited.

PY - 2023

Y1 - 2023

N2 - Membrane-less organelles assemble through liquid–liquid phase separation (LLPS) of partially disordered proteins into highly specialized microenvironments. Currently, it is challenging to obtain a clear understanding of the relationship between the structure and function of phase-separated protein assemblies, owing to their size, dynamics and heterogeneity. In this Perspective, we discuss recent advances in mass spectrometry (MS) that offer several promising approaches for the study of protein LLPS. We survey MS tools that have provided valuable insights into other insoluble protein systems, such as amyloids, and describe how they can also be applied to study proteins that undergo LLPS. On the basis of these recent advances, we propose to integrate MS into the experimental workflow for LLPS studies. We identify specific challenges and future opportunities for the analysis of protein condensate structure and function by MS.

AB - Membrane-less organelles assemble through liquid–liquid phase separation (LLPS) of partially disordered proteins into highly specialized microenvironments. Currently, it is challenging to obtain a clear understanding of the relationship between the structure and function of phase-separated protein assemblies, owing to their size, dynamics and heterogeneity. In this Perspective, we discuss recent advances in mass spectrometry (MS) that offer several promising approaches for the study of protein LLPS. We survey MS tools that have provided valuable insights into other insoluble protein systems, such as amyloids, and describe how they can also be applied to study proteins that undergo LLPS. On the basis of these recent advances, we propose to integrate MS into the experimental workflow for LLPS studies. We identify specific challenges and future opportunities for the analysis of protein condensate structure and function by MS.

U2 - 10.1038/s41596-023-00900-0

DO - 10.1038/s41596-023-00900-0

M3 - Journal article

C2 - 37907762

AN - SCOPUS:85175473079

VL - 18

SP - 3653

EP - 3661

JO - Nature Protocols

JF - Nature Protocols

SN - 1754-2189

ER -

ID: 372325404