Department of Microbiology & Immunology Seminar: “Multiprotein Assemblies: Dynamic Behavior”
Speaker:
Natalya Kurochkina, PhD
Professor, Department of Biophysics
The School of Theoretical Modeling, Washington, DC
Location: Med-Dent NE301 and via Zoom
Abstract:
Proteins are remarkably regular objects. They perform their functions with high precision which we attribute to underlying structural principles. Noncovalent interactions of protein atomic groups exhibit regularities that guide fold of the molecule and assembly of multiprotein complexes and their ligands. Characteristic pattern of contacts derived for the calcium sensor molecule calmodulin reveals how calmodulin mimics its ligands and what key factors contribute to its parallel/antiparallel orientation, accessibility to kinases/phosphatases and functional states. Calmodulin plays a crucial role in calcium signaling pathways including those involved in response to injury, inflammation, or viral infection and represents an attractive target for the design of new therapies.