Abstract
The condensation of proteins with low complexity sequences plays both functional and pathogenic roles in living cells. Recent efforts to understand the chemistry of biomolecular condensates have revealed that protein sequences harboring weak and dynamic multivalent interaction sites produce the macroscopic behavior observed in living cells. The hydrogen bonding, cation-π, π-π, dipole-dipole, and cation-anion interactions involved are well understood individually, yet fundamental and intriguing questions remain regarding how this chemistry works in specific biological contexts at the structural level.
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