The
daunting challenge in the era of proteomics is to identify the
functions of all the proteins identified by the Genomic Project and to
elucidate the interplay among these proteins in governing the normal
activities of organisms. One approach is to define the structural folds
of these proteins. However, a meaningful structure-function correlation
depends on an understanding of the unique properties associated with
these structural folds. We are studying various folds, namely, the TIM
barrel which is the basic fold of hundreds of enzymes; the PDZ fold
involved extensively in signal transduction; the globulin fold in viral
envelop proteins and the helix-turn-helix motif adopted by many DNA
binding proteins. The approaches are biophysical solution chemistry in
conjunction with structural biology, computation chemistry and molecular
biology.
Search PubMed for Dr. Lee's publications.