Dr. Vince  J.  LiCata   is currently working as a Louis S. Flowers Professor  in the Department of Department of Biological Sciences, Louisiana State University , USA. His research interests includes protein systems, including HIV reverse transcriptase, Deinococcus radiodurans Pol I polymerase, Rec A, the mammalian adipocyte lipid binding protein (ALBP), and aspartate transcarbamylase. He is serving as an editorial member and reviewer of several international reputed journals. Dr. Vince  J.  LiCata   is the member of many international affiliations. He has successfully completed his Administrative responsibilities. He has authored of many research articles/books related to protein systems, including HIV reverse transcriptase, Deinococcus radiodurans Pol I polymerase, Rec A, the mammalian adipocyte lipid binding protein (ALBP), and aspartate transcarbamylase.

Our laboratory studies proteins: most particularly protein-DNA and protein-ligand interactions, protein folding and stability, and protein structure and conformation in solution. Our work is primarily focused on the Type I DNA polymerases from Thermus aquaticus (Taq/Klentaq) and E. coli (Pol I/Klenow). The DNA polymerases from E. coli and T. aquaticus are a homologous mesophilic-thermophilic pair of proteins. Their molecular structures and basic catalytic functions are highly homologous, yet the Taq enzyme works near the boiling point of water, while the E. coli enzyme is irreversibly destroyed by exposure to 50oC. We directly and comparatively examine the DNA binding, protein folding, and global structural characteristics of these two species of DNA polymerases with the goal of delineating the exact differences and similarities between the two proteins in order to understand what features are necessary to achieve high temperature stability and activity for a DNA polymerase. These studies include characterizations of DNA binding using fluorescence anisotropy and titration calorimetry, characterizations of stability using thermal and chemical denaturation methods, and characterization of structural and conformational changes using small angle X-ray scattering, and analytical ultracentrifugation. We also examine similar questions in other protein systems, including HIV reverse transcriptase, Deinococcus radiodurans Pol I polymerase, Rec A, the mammalian adipocyte lipid binding protein (ALBP), and aspartate transcarbamylase