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.
I: Nature Protocols, Bind 18, 2023, s. 3653–3661.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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