Research Focus

My research focuses on understanding the how transcription factors and enzymes modify their conformation and partnerships upon receiving signals. These signals may include the binding of ligands or post-translational modifications such as phosphorylation. Nuclear magnetic resonance (NMR) spectroscopy is routinely used to determine atomic-level structures of the protein complexes studied in the laboratory. All of projects undertaken in the laboratory are very collaborative and have molecular biological and biochemical components that complement the NMR studies. As structural studies also have a computational component, a willingness to use computers (UNIX-based systems) is a must.

Representative Publications

Smirnova E, Shanbhag R, Kurabi A, Mobli M, Kwan JJ, Donaldson LW. (2013). Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein. PLoS One. 14(8)

Kwan JJ, Smirnova E, Khazai S, Evanics F, Maxwell KL, Donaldson LW. (2013). The Solution Structures of Two Prophage Homologues of the Bacteriophage λ Ea8.5 Protein Reveal a Newly Discovered Hybrid Homeodomain/Zinc-Finger Fold. Biochemistry. 52(21)

Alipanahi B , Krislock N , Ghodsi A , Wolkowicz H , Donaldson L , Li M. (2013). Determining protein structures from NOESY distance constraints by semidefinite programming.Journal of Computational Biology 20(4)

Alipanahi B , Gao X , Karakoc E , Li SC , Balbach F , Feng G , Donaldson L , Li M. (2011). Error tolerant NMR backbone resonance assignment and automated structure generation.Journal of Bioinformatics and Computational Biology. 9(1)

Pell LG Gasmi-Seabrook GM Morais M Neudecker P Kanelis V Bona D Donaldson LW Edwards AM Howell PL Davidson AR. (2010). The solution structure of the C-terminal Ig-like domain of the bacteriophage λ tail tube protein. J Mol Biol. 403(3).

Sub-Disciplines

Cell Biology, Protein Biochemistry, Structural Biology

Research Areas