Intrinsically disordered proteins, which don’t have just one three-dimensional structure, often carry out their biological roles through transition between structures. For example, a pH-dependent change in condensation effects iridescence in squid proteins; a selection of competing folded conformations drive neurodegeneration-related condensation of TDP53; and a transition from closed to open structure controls protease sensitivity of an enzyme important for asthma and allergies.
The talks in this virtual event were originally programmed to take place as an in-person Spotlight Session at the 2020 ASBMB Annual Meeting.
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