Although, I received my Ph.D from MIT in 2004 for studying protein folding and aggregation, my true passion has always been in biology teaching and education. I was an education research post doc for two years in the HHMI Education Group at MIT and focused primarily on biological education research and the importance of concept-based teaching and learning in biology.

I have recently recognized the need for better biological preparation at the high school level and am actively involved in several secondary education efforts. I am currently a faculty advisor to the United States Biology Olympiad Team involved in exam preparation, student advising and instruction, and program redesign. I am also involved in counseling area high school biology teachers in methods to incorporate college level molecular biology labs into their classrooms.

In light of my interest in protein structure, I am studying the importance of learning and manipulation of biological macromolecules in 3-dimensions. I am currently part of a collaboration with the Biology, Physics, and Academic Computing Departments at MIT to create a free, scalable 3D visualization software engine that may easily be manipulated by students, but has the flexibility and functionality to be used by advance protein biochemists. I am hoping to incorporate this program into the Brandeis curriculum.

Here at Brandeis, I am teaching the introductory biology lab course and a graduate level molecular biology course. I hope to incorporate elements of protein folding and aggregation studies into the introductory biology laboratory and to mentor undergraduate and graduate students biology students interested in pursuing teaching careers.

Publications:

Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin. Mills IA, Flaugh SL, Kosinski-Collins MS, King JA. Protein Sci. 2007 Nov;16(11):2427-44. Epub 2007 Sep 28. [abstract]

Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability. Flaugh SL, Kosinski-Collins MS, King J. Protein Sci. 2005 Aug;14(8):2030-43. [abstract]

Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. Flaugh SL, Kosinski-Collins MS, King J. Protein Sci. 2005 Mar;14(3):569-81. [abstract]

The role of the hydrophilic interface residues in folding and aggregation of human gammaD crystallin. Flaugh, S.L., Kosinski-Collins, M.S., & King, J.A. 2005. Protein Sci. 14: 2030-2043.

The role of the hydrophobic interface residues in folding and stability of human gammaD crystallin. Flaugh, S.L., Kosinski-Collins, M.S., & King, J.A. 2005. Protein Sci. 14: 569-581.

Probing folding and fluorescence quenching in human gammaD crystallin Greek key domains using triple tryptophan mutant proteins. Kosinski-Collins M.S., Flaugh S.L., King J. (2004) Protein Science. 13: 2223-35. [abstract]

In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation. Kosinski-Collins, M.S. & King, J.A. 2003. Protein Sci. 12: 480-90. [abstract]

 

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Last review: July 16, 2009.