The first step in unfolding EnHD is helix III pulling away from helices I and II and exposing the hydrophobic core.

I am a fourth-year graduate student in the Biomolecular Structure and Design Program at the University of Washington in Seattle. I work in the Daggett Lab on protein folding.

I'm studying the model protein, engrailed homeodomain (EnHD), since it is an ultra-fast folding and unfolding protein and its folding/unfolding dynamics have been extensively characterized both experimentally and computationally. This is important because molecular dynamics (MD) can currently only probe protein motion on scales up to microseconds. Using the lab's extensive set of MD analysis tools, I am able to analyze the folding and unfolding pathway of the protein under a variety of different conditions.

Curriculum Vitae

Publications

• Bean GJ, Flickinger ST, Westler W, McCully ME, Sept D, Weibel DB, Amann KJ. A22 disrupts the bacterial actin cytoskeleton by directly binding and inducing a low-affinity state in MreB. Biochemistry. 48(22): 4852-7, 2009. [DOI]
• McCully ME, Beck DAC, Daggett V. Microscopic reversibility of protein folding in molecular dynamics simulations of the engrailed homeodomain. Biochemistry. 47(27): 7079-89, 2008. [DOI]
• Kim K, McCully ME, Bhattacharya N, Butler B, Sept D, Cooper JA. Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actin-capping protein: implications for how capping protein binds the actin filament. J Biol Chem. 282(8): 5871-9, 2007. [DOI]

e-mail: mmccully (at) u.washington.edu
lab: 206 543 9305