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Skidmore College
Chemistry Department
Madushi Raththagala

Madushi Raththagala

Assistant Professor of Chemistry

Office: Dana 218
Phone: 518-580-8193
Fax: 518-580-5129


  • B.Sc. (Honors) Biochemistry and Molecular Biology 2002, University of Colombo, Sri Lanka

  • Ph.D. Chemistry 2008, Michigan State University

  • Postdoctoral Researcher, Johns Hopkins University, 2010-2012

  • Postdoctoral Researcher, University of Kentucky, 2012-2017  

At Skidmore since 2017



Our research interests emphasize the general area of structural biochemistry, using biophysical and biochemical approaches to characterize proteins involved in reversible phosphorylation of carbohydrates. We are particularly interested in understanding the molecular mechanisms by which glucan phosphatase Starch Excess4 regulate starch phosphorylation in plant systems. Starch Excess4 is essential for starch degradation and its absence leads to accumulation of starch granules in plant leaves.

Current studies focus on unraveling the mechanistic details of position specific activity of Starch Excess4. One of the major challenges of studying Starch Excess4 is defining it in the complex starch structure. Focusing on specific starch engagement and activity, students in my group will employ a variety of biophysical techniques including x-ray crystallography, small angle x-ray scattering, and differential scanning fluorimetry to study Starch Excess4. Our efforts are to remove the key gaps in knowledge in reversible starch phosphorylation with the hope of developing a new strategy to utilize starch in an industrial setting and future biofuel research.


  • CH341 Biochemistry: Macromolecular Structure and Function with Lab


  • Carlos Roma-Mateo, Madushi Raththagala, Matthew S. Gentry, Pascual Sanz. Assessing the biological activity of the glucan phosphatase laforin. Methods in Molecular Biology, 2016, 1447:107-19. 
  • Casper Wilkens, Kyle D. Auger, Nolan T. Anderson, Madushi Raththagala, M. Abou Hachem, Christina M. Payne, Matthew S. Gentry, Birte Svensson. Plant α-glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose. FEBS Letters, 2016, Jan;590(1):118-28.
  • Madushi Raththagala, Mary K. Brewer, Matthew W. Parker, Amanda R. Sherwood, Brian K. Wong, Simon Hsu, Travis M. Bridges, Bradley C. Paasch, Lance C. Hellmen, Satrio Husodo, Adam O. Taylor, Benjamin D. Turner, Kyle D. Auger, Vikas V. Dukhande, Srinivas Chakrawarthy, Pascual Sanz, Virgil V. Woods, Sheng Li, Craig W. Vander Kooi, Matthew S. Gentry. Structural mechanism of laforin function in glycogen dephosphorylation and Lafora disease, Molecular Cell, 2015, Jan;22;57(2):261-72.
  • David A. Meekins, MadushiRaththagala, Kyle D. Auger, Benjamin D. Turner, Dianna Santelia, Oliver Kötting, Matthew S. Gentry, Craig W. Vander Kooi. Mechanistic insights into glucan phosphatase activity against polyglucan substrates. Journal of Biological Chemistry, 2015, Sep;18;290(38):23361-70.
  • Nicholas Clark, Madushi Raththagala, Nathan T. Wright, Elizabeth A. Buenger, Joel F. Schildbach, Susan Krueger, Joseph E. Curtis. Solution structure of TraI in solution. Journal of Molecular Modeling, 2014, Jun;20(6):2308
  • David A. Meekins, Madushi Raththagala, Satrio Husodo, Cory J. White*, Hou fu Guo, Oliver Kötting, Craig W. Vander Kooi, Matthew S. Gentry. Phosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals the mechanism for C6 specificity, Proceedings of National Academy of Sciences USA (PNAS), 2014, 20;111(20):7272-7
  • Pascual Sánchez-Martín, MadushiRaththagala, Travis M. Bridges, Satrio Husodo, Matthew S. Gentry, Pascual Sanz, Carlos Romá-Mateo. Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329. PLoS One, 2013, Jul 26;8(7):e69523
  • Nathan T. Wright, Madushi Raththagala, Casey W. Hemmis, Sheldon Edwards, Joseph E. Curtis, Susan Krueger, Joel F. Schildbach. Solution structure and small angle scattering analysis of TraI (381-569). Proteins, 2012, Aug;80(9):2250-61.
  • Madushi Raththagala, Welivitiya Karunarathne, Mark Kryziniak, John McCracken, Dana M. Spence. Hydroxyurea stimulates the release of ATP from rabbit erythrocytes through an increase in calcium and nitric oxide production. European Journal of Pharmacology, 2010, Oct 25;645(1-3):32-8.
  • Nicole V. Tolan, Luiza I. Genes, Chintha W. Subasinghe, Madushi Raththagala, Dana M. Spence. Personalized metabolic assessment of erythrocytes using microfluidic delivery to an array of luminescent wells. Analytical Chemistry,2009 15;78(24):8556-60.
  • Madushi Raththagala, Paul D. Root, Dana M. Spence. Dynamic monitoring of glutathione in erythrocytes, without a separation step, in the presence of an oxidant insult. Analytical Chemistry, 2006,15;78(24):8556-60.
  • Jamie Carroll, Madushi Raththagala, Chintha W. Subasinghe, Stacy Baguzis, Teresa D’amico Oblak, Paul Root, Dana M. An altered oxidant defense system in red blood cells affects their ability to release nitric oxide-stimulating ATP. Molecular Bio systems, 2006, Jun;2(6-7):305-11.


  • American Association for the Advancement of Science (AAAS)
  • American Chemical Society (ACS)
  • American Society of Biochemistry and Molecular Biology