Using solid-state NMR to study protein clumping, phase changes, and droplet-like assemblies

Solid-state nuclear magnetic resonance (NMR) spectroscopy offers multiple methods to study diverse protein assemblies and their dynamics.

• Biomolecular condensates play crucial roles in various cellular processes such as immune signaling, mRNA transport, and autophagy.
• Phase-separated condensates may contribute to protein misfolding and aggregation, which are linked to neurodegenerative diseases.
• Protein phase separation involves the creation of complex and dynamic structures that can transition into gel-like or semi-crystalline forms.
• High-resolution structural biology techniques face challenges in characterizing these heterogeneous assemblies.
• The review discusses the applicability of solid-state NMR techniques for investigating protein condensates and the dynamics of phase transitions.

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