Solid-state NMR methods to investigate biomolecular condensates, protein phase transition, phase separation and coacervates
Abstract
The formation of biomolecular condensates has been linked to a broad range of essential cellular processes, including immune signaling cascades, mRNA transport, and autophagy. Conversely, phase-separated condensates have also been associated with aberrant protein misfolding and subsequent aggregation in neurodegenerative disease-related processes. Protein phase separation and phase transitions involve the formation of heterogeneous and dynamic assemblies that can evolve into gel-like or semi-crystalline states, which are challenging to characterize using high-resolution structural biology techniques. Solid-state nuclear magnetic resonance (NMR) spectroscopy now offers a broad arsenal of methods to probe the structural and dynamic features of viscous condensates, elastic solids, coacervates and rigid protein assemblies. This review provides an overview of solid-state NMR approaches that are readily applicable and discusses potential methodological developments to investigate protein condensates and coacervates as well as to study protein phase separation and phase transitions.
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BibTeX
@article{deb2026solidstate,
title = {{Solid-state NMR methods to investigate biomolecular condensates, protein phase transition, phase separation and coacervates}},
author = {Seamoon Deb and Erick Dufourc and Birgit Habenstein and Sven Saupe and Antoine Loquet},
journal = {Biophysical Chemistry},
year = {2026},
month = oct,
doi = {10.1016/j.bpc.2026.107692},
url = {https://hal.science/hal-05842104v1},
note = {CC BY-NC},
}
RIS
TY - JOUR
TI - Solid-state NMR methods to investigate biomolecular condensates, protein phase transition, phase separation and coacervates
AU - Seamoon Deb
AU - Erick Dufourc
AU - Birgit Habenstein
AU - Sven Saupe
AU - Antoine Loquet
PY - 2026
DA - 2026/10/28
JO - Biophysical Chemistry
DO - 10.1016/j.bpc.2026.107692
UR - https://hal.science/hal-05842104v1
AB - The formation of biomolecular condensates has been linked to a broad range of essential cellular processes, including immune signaling cascades, mRNA transport, and autophagy. Conversely, phase-separated condensates have also been associated with aberrant protein misfolding and subsequent aggregation in neurodegenerative disease-related processes. Protein phase separation and phase transitions involve the formation of heterogeneous and dynamic assemblies that can evolve into gel-like or semi-crystalline states, which are challenging to characterize using high-resolution structural biology techniques. Solid-state nuclear magnetic resonance (NMR) spectroscopy now offers a broad arsenal of methods to probe the structural and dynamic features of viscous condensates, elastic solids, coacervates and rigid protein assemblies. This review provides an overview of solid-state NMR approaches that are readily applicable and discusses potential methodological developments to investigate protein condensates and coacervates as well as to study protein phase separation and phase transitions.
SN - 0301-4622
ER -