University of Minnesota
School of Physics & Astronomy
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Mark Rustad

PAN 417 (office)
NHH 5-290 (lab)
rustad @

Summary of Interests
Calcium transport in heart cells; Electron Paramagnetic Resonance (EPR); Molecular Dynamics (MD) Simulations [Research Web Page]

About My Work

The sarco(endo)plasmic reticulum calcium ATPase (SERCA) transports calcium from the cytosol into the lumen of the sarcoplasmic reticulum after muscle contraction. It is known that physiological problems arise in living systems if calcium concentrations in cells are improperly regulated; various types of heart disease are linked to improper SERCA activity. A newly discovered peptide named dwarf open reading frame (DWORF) has been found to play a role in the regulation of calcium ion concentration in muscle cells in both vertebrates and invertebrates. Specifically, DWORF enhances the activity levels of SERCA by interacting with SERCA-inhibitors: phospholamban (PLB), sarcolipin (SLN), and myoregulin (MLN) in vertebrates; and sarcolamban A and B (sclA and sclB) in invertebrates. It is important to understand the mechanism of interaction between DWORF, SERCA, and inhibitors of SERCA due to the correlation of heart disease and insufficient DWORF production in people and animals. Ischemic failing human hearts showed severe down-regulation of DWORF, and similarly, mice with hypertrophic heart disease exhibit down-regulation of DWORF as well.

I use electron paramagnetic resonance (EPR) spectroscopy to investigate the mechanism of interaction of DWORF with SERCA, and inhibitors of SERCA. EPR is an experimental technique that utilizes the absorbance of magnetic fields by paramagnetic molecular probes attached to proteins to provide orientationally, structural and dynamical information of proteins and protein complexes. Continuous wave electron paramagnetic resonance (CWEPR) can probe protein interactions that occur on time scales ranging from picoseconds to hundreds of nanoseconds (10-12 to 10-7 s) while saturation transfer electron paramagnetic resonance (STEPR) can investigate protein dynamics on slower time scales on the order of milliseconds (10-3 s).

Selected Publications

Mark Rustad, Allen Eastlund, Ryan Marshall, Paul Jardine, Vincent Noireaux, Synthesis of Infectious Bacteriophages in an E. coli-based Cell-free Expression System, Journal of Visualized Experiments [abstract] [download 2017-Synthesis_of_Infectious_Bacteriophages_in_an_E._coli-ba]

Garamella, Jonathan Marshall, Ryan Rustad, Mark Noireaux, Vincent, The All E. coli TX-TL Toolbox 2.0: A Platform for Cell-Free Synthetic Biology, ACS Synthetic Biology [abstract] [download 2016-The_All_E._coli_TX-TL_Toolbox_2.0_A_Platform_for_Cell-F]

Mark Rustad and Kingshuk Ghosh, Why and how does native topology dictate the folding speed of a protein?, Journal of Chemical Physics [abstract] [download 2012-Why_and_how_does_native_topology_dictate_the_folding_sp]


B.Sc. Physics and Mathematics, University of Denver (2011)
M.Sc. Physics, University of Minnesota (2014)