Marassi Lab
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Our Lab focuses on understanding the structures and functions of proteins embedded in cellular membranes. Membrane proteins mediate all interactions of a cell or organism with the outside world and, as such, are responsible for the basic human experiences (taste, smell, touch, sight, thought, etc.) that constitute life. They are encoded by at least 30 percent of all genes and perform essential biological functions that include cellular transport, signaling, and programmed cell death. Dysfunctions of human membrane proteins are linked with devastating diseases and the membrane proteins encoded by viruses and bacteria play major roles in infection, virulence, and antibiotic resistance. It is, therefore, not surprising that membrane proteins are the principal targets of most drugs on the market today and that understanding their biological functions is a major goal of biomedical research.
The three-dimensional structure of a protein is essential for understanding its mechanisms of action, for medicinal chemistry efforts, and for the development of therapies. Dr. Marassi’s primary research tool is NMR spectroscopy, a powerful technique that utilizes strong magnetic fields to extract structural information from biological molecules and characterize their interactions with their cellular partners. Her laboratory uses complementary approaches of solution NMR and solid-state NMR for proteins that are embedded in lipid bilayers to obtain direct information about three-dimensional structure and membrane orientation.
Our Research is supported by the National Institutes of Health.
We are working to understand how proteins on the surface of pathogenic bacteria interact with the human host to promote cell adhesion/invasion, evade host immunity, and enhance pathogen survival and proliferation.
Suppression of programmed cell death, is a hallmark of cancer. We are working to understand how proteins in the B-cell -leukemia-lymphoma family regulate apoptosis at intracellular membranes.
We are working to understand the molecular basis of protein aggregates that collectively form the plaques associated with age-related macular degenration, Alzheimer's disease, Atherosclerosis and related diseases.
NMR structure determination is uniquely suited for samples that are close to native conditions. We are developing an implicit solvation potential for NMR-restrained protein structure calculationss in physically realistic water and water-membrane environments.