Proteins are folded into specific three dimensional (3D) structures. These structures are essential for imparting functions such as molecular recognition and catalysis. Without a precise knowledge of their 3D-structures, we are unable to understand how proteins execute their respective molecular functions. It is virtually impossible to predict protein 3D-structures from amino acid sequences alone. Thus, the experimental determination of protein 3D-structures represents the hallmark of structural biology. Structural biology in our laboratory is performed using X-ray crystallography to determine the 3D-structures of proteins and molecular complexes at atomic resolution, and biochemical/biophysical analyses are performed to delineate the mechanisms by which proteins function at the atomic, molecular and cellular levels.
Our general goal is to contribute towards our understanding of the nature of life. Our long-term objective is to understand the molecular functions of proteins and other biological macromolecules and their complexes in terms of molecular structures. Our efforts are directed towards defining the manner by which protein interactions and 3D-structures determine specificity and how structural changes enable functional switches in living cells.