Intrinsically disordered proteins

July 7, 2020 | Duration: 51 mins.

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.


Chair: Robert Levenson

Charge neutralization tunes dynamic arrest of initially disordered reflectin proteins
Robert Levenson, University of California, Santa Barbara

Competing modes of assembly restrict amyloid formation by a neurodegenerative protein, TDP43
Jianzheng Wu, Stowers Institute for Medical Research

Elucidating the open and active conformation of human 5-Lipoxygenase
Eden Gallegos, Louisiana State University