Speaker
Atrayee Sarkar
(University of Houston)
Description
Mutations in the Superoxide Dismutase 1 (SOD1) protein may cause misfolding and aggregation leading to the neurodegenerative disease ALS. Despite numerous studies a clear understanding of the impact of electrostatics and crowding on the folding and aggregation of SOD1 remains lacking. In this work, we use a structure-based model and molecular dynamics simulation to study the effects of electrostatics on SOD1 folding in a crowded environment. We show that electrostatics affect the unfolded protein configurations more significantly than the folded ones. Using a new order parameter, we suggest the presence of an intermediate state and show that electrostatics play an important role in the folding pathway of SOD1.
| Academic year | 5th year and/or beyond |
|---|---|
| Research Advisor | Dr. Greg Morrison |
Author
Atrayee Sarkar
(University of Houston)
Co-authors
Dr
Andrei G. Gasic
(Center for Theoretical Biological Physics, Rice University)
Dr
Margaret S. Cheung
(Pacific Northwest National Laboratory, Seattle Research Center, Seattle)
Dr
Greg Morrisson
(University of Houston; Center for Theoretical Biological Physics, Rice University)
