Thus a knowledge of the mechanisms of protein interactions is not only relevant to biology but its impact on medicine will be even greater. The better we understand how these molecular motors function, the better we will be equipped to design and develop novel genetic and pharmaceutical therapies to combat disease. One approach directed towards unraveling the mechanisms of protein interactions is to study proteins at structural level, or in terms of their shapes. For example, the shapes of the various parts of a mechanical engine such as the piston, the wheels and the gears lend ample information about the way it is driven. In a similar manner, the shapes of proteins and their interactands hold clues to the way they execute their biological activity. Unraveling the molecular mechanisms of protein interactions will be the biggest challenge of the post-genomic era in the twenty first century. It is towards this goal that our research efforts, using heteronuclear multi-dimensional NMR in conjunction with other biophysical, biochemical and molecular biological techniques, largely focus on. The realization that structure per se does not hold all the clues to the highly flexible nature of proteins has prompted us not to be merely interested in determining static structures but rather study changes in structure as a function of time in response to specific biological demands and relate such changes to dynamic, thermodynamic and kinetic properties of biological systems. For further information, please visit farooqlab.net.

Representative Publications

1.    Zhang Q, Muller M, Chen CH, Zeng L, Farooq A & Zhou MM (2005). New Insights into the Catalytic Activation of the MAPK Phosphatase PAC-1 Induced by its Substrate MAPK ERK2 Binding. Journal of Molecular Biology 354, 777-788.

2.    Sudol M, Recinos CC, Abraczinkas J, Humbert J & Farooq A (2005). WW or WoW — The WW Domains in a Union of Bliss. IUBMB Life 57, 773-778.

3.    Qian C, Wang X, Manzur K, Sachchidanand, Farooq A, Zeng L, Wang R & Zhou MM (2006). Structural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferase. Journal of Molecular Biology 359, 86-96.

4.    Farooq A, Sudol M & Zhou MM (2006). Two Is Better Than One — Structure, Function and Mechanism of Protein Domains Acting in Tandem. In “Focus on Cellular Signaling Research”, Leeds DT editor, Nova Publishers; Chapter 5, 117-136.

5.    Ramsauer VP, Pino V, Farooq A, Carraway CAC, Salas PJI & Carraway KL (2006). Muc4-ErbB2 Complex Formation and Signaling in Polarized CACO-2 Epithelial Cells Indicate That Muc4 Acts as an Unorthodox Ligand for ErbB2. Molecular Biology of the Cell 17, 2931-2941.