Shape shifting in the control of protein function
What roles do conformational changes play in regulating protein function? Protein shape change can be triggered by a variety of factors, including ligand binding, temperature or pH, and can alter enzyme activity and function, allowing enzymes to carry out different functions in different contexts. In this virtual event, researchers present their findings on proteins that undergo conformational changes including reassembly, oligomerization and fold-switching.
The talks in this virtual event were originally programmed to take place as an in-person Spotlight Session at the 2020 ASBMB Annual Meeting.
Talks
Chair: Eileen Jaffe
Multimeric proteins that can come apart, change shape and reassemble differently with functional consequences — morpheeins
Eileen Jaffe, Fox Chase Cancer Center
Filament formation induces a shape change and activation of the nuclease SgrAI
Nancy Horton, University of Arizona
Fold-switching sets the stage for cooperativity and competition in the cyanobacterial circadian clock
Carrie Partch, University of California, Santa Cruz
Dynamic oligomerization in Burkholderia cenocepacia HMG-CoA reductase
Jeffrey Watson, Gonzaga University
Moonlighting proteins where changing shape promotes changing function
Constance Jeffery, University of Illinois, Chicago
Who should watch
- Graduate students
- Postdocs
- Staff scientists
- PIs
- Researchers interested in enzyme regulation through conformational change
Key takeaways
Attendees will learn how a variety of conformational changes control and alter protein function through presentations on recent research in the field.