Francesca Marassi, Ph.D, Medical College of Wisconsin, Professor, Chair, and Eminent Scholar; Associate Director, MCW Cancer Center Shared Resources, "Biological insights from NMR of lipid-protein assemblies in situ"

Date and Time
Location
ESB 1001
Francesca Marassi, Ph.D
Francesca Marassi, Ph.D

Speaker:

Francesca Marassi, Ph.D.

Professor, Chair, and Eminent Scholar; Associate Director, MCW Cancer Center Shared Resources

Medical College of Wisconsin

Faculty Host: Dorit Hanein

 

Title:  Biological insights from NMR of lipid-protein assemblies in situ

 

Abstract: 

The direct analysis of proteins in their native environment has long been a goal of structural biology and a major driver of technology development in nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR), and electron microscopy (EM). The importance of environmental effects on protein structure has been appreciated for some time, and underpins the development of approaches that enable structural biology studies in situ. 

NMR is very well suited for in situ structural studies. This talk will review recent advances in NMR that enable structural and functional analyses of protein-lipid assemblies associated with host pathogen interactions and diseases of aging, in native samples. 

Bio:

Francesca Marassi is a Professor and Chair of the Department of Biophysics at the Medical College of Wisconsin and her research focuses on understanding the molecular bases for protein-lipid interactions in biological processes associated with bacterial infections and diseases of aging. A central philosophy of her research is to work within native bacterial membranes to gain insights that are directly translatable to the physiological environment, and her laboratory has focused on developing and applying NMR spectroscopy for this purpose. She has more than 30 years of experience with the experimental and computational aspects of nuclear magnetic
resonance (NMR) including methods development and biomolecular applications. Her lab uses the complete array of solution and solid-state NMR methods to study proteins in multi-component assemblies with varying degrees of dynamics and focus increasingly on native cellular or sub-cellular samples to establish authentic structure- activity correlations. Their multidisciplinary approach also includes X-ray crystallography, electron microscopy, molecular dynamics simulations, biochemistry and cell biology. This allows them to probe structure and activity across the scales of dimension and time relevant for human biology. Her research is described in more than 100 peer-reviewed publications.