Marissa Saunders received her B.Sc.(hons) in Biochemistry in 2006 from the University of Pretoria. She joined the Voth group in 2006 after a brief rotation in the lab. In 2012, she received her PhD from the University of Chicago for the work that she has done in using molecular dynamics and coarse-grained analysis to better understand the dynamics of actin, an important cytoskeletal protein. She is currently working as a postdoc in the Voth lab and is currently engaged in developing coarse-grained models for actin networks as part of the NSF-funded Center for Multiscale Theory and Simulation. This work involves significant collaboration with other theory groups at the University of Chicago, including the Hinrichs, Roux, Freed, and Dinner groups.
I am interested in understanding how small scale changes in atomistic structure can be related to large-scale changes in structure, function, and material properties in biophysical systems. My research focuses on the actin, a cytoskeletal protein that is dynamically organized into diverse network architectures within the cell. These networks function to promote cell mobility, intracellular trafficking, and muscle contraction. To understand how these functions are related to the atomistic details of individual actin subunits, including the nucleotide bound at the cleft of each actin protein, I utilize a multiscale analytical approach in which information from molecular dynamics simulations is used to identify slow collective motions within actin subunits and within actin filaments. Based on the changes in these slow motions induced by changing, for example, ATP to ADP, we can start to understand the connection between scales and build coarse-grained models of the actin filament that accurately capture the important underlying atomistic physics of the system.
- Saunders, M. G. & Voth, G. A. (2012). Comparison between actin filament models: coarse-graining reveals essential differences. Structure 20, 641-653.
- Saunders, M. G. & Voth, G. A. (2012). Coarse-graining of multiprotein assemblies. Curr Opin Struct Biol 22, 144-150.
- Saunders, M. G. & Voth, G. A. (2011). Water molecules in the nucleotide binding cleft of actin: effects on subunit conformation and implications for ATP hydrolysis. J. Mol. Bio. 413, 279-291
- Sinitskiy, A. V., Saunders, M. G. & Voth, G. A. (2012). Optimal Number of coarse-grained sites in different components of large biomolecular complexes. J. Phys. Chem. B. Articles ASAP, doi: 10.1021/jp2108895.
- Fan, J., Saunders, M. G. & Voth, G. A. (2012). Coarse-graining provides insights on the essential nature of heterogeneity in actin filaments. Biophys. J. under review
- Maupin, C. M., Saunders, M. G., Thorpe, I. F., McKenna, R., Silverman, D. N. & Voth, G. A. (2008). Origins of Enhanced Proton Transport in the Y7F Mutant of Human Carbonic Anhydrase II. JACS130, 11399-11408.