Hosted by: Silvia Ramundo
A new-found interest in the field of protein science has focused on the capacity of certain proteins to polymerize into labile, cross- fibrils. Formation of labile polymers has been observed for proteins that utilize only a small subset of the 20 amino acids normally required for protein folding. When incubated in isolation at neutral pH and physiologic ionic strength, these “low complexity” (LC) protein sequences polymerize into amyloid-like fibers. Unlike pathologic amyloids, LC domain polymers dissolve upon dilution. It has been hypothesized that this form of reversible polymerization may play a foundational role in the organization of intracellular puncta not surrounded by investing membranes.